SitesBLAST
Comparing Ga0059261_1577 FitnessBrowser__Korea:Ga0059261_1577 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
43% identity, 98% coverage: 5:463/470 of query aligns to 1:452/456 of 5oqtA
- binding alanine: I38 (= I40), G40 (= G42), T41 (= T43), G42 (= G44), F226 (= F237), A227 (= A238), I229 (≠ Y240)
- binding : E24 (≠ T26), G26 (≠ S28), F28 (≠ P30), D29 (≠ H31), M32 (≠ A34), A176 (= A177), R177 (≠ T178), A184 (≠ V185), A188 (≠ I189), L192 (≠ V193), Q294 (≠ R306), V297 (≠ F309)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
43% identity, 98% coverage: 4:463/470 of query aligns to 2:454/458 of 6f34A
- binding arginine: I40 (= I40), G42 (= G42), T43 (= T43), G44 (= G44), E115 (= E114), Y116 (= Y115), A119 (≠ V118), F228 (= F237), A229 (= A238), I231 (≠ Y240), V314 (= V324)
- binding cholesterol: W201 (≠ P200), Y202 (= Y201)
- binding : G28 (≠ S28), F30 (≠ P30), D31 (≠ H31), M34 (≠ A34), A178 (= A177), R179 (≠ T178), A186 (≠ V185), I187 (≠ V186), A190 (≠ I189), L194 (≠ V193), Q296 (≠ R306), V299 (≠ F309)
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
33% identity, 86% coverage: 9:413/470 of query aligns to 16:439/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 91% coverage: 37:463/470 of query aligns to 14:430/433 of 6f2wA
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
24% identity, 76% coverage: 17:371/470 of query aligns to 5:346/457 of P15993
- Y103 (= Y115) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
24% identity, 84% coverage: 12:407/470 of query aligns to 10:394/458 of P24207
- R26 (≠ P30) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P58) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (≠ A91) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y94) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y96) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ V98) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L99) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ I102) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ W105) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W109) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ L111) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ I112) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y115) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ S120) mutation E->G,L,V,N: Loss of activity.
- K168 (= K187) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D243) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ A269) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P358) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
Sites not aligning to the query:
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
20% identity, 86% coverage: 17:419/470 of query aligns to 2:399/469 of P46349
- G33 (≠ L48) mutation to D: Lack of activity.
- G42 (= G57) mutation to S: Lack of activity.
- G301 (≠ F328) mutation to V: Lack of activity.
- G338 (vs. gap) mutation to E: Lack of activity.
- F341 (≠ T365) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 88% coverage: 13:427/470 of query aligns to 8:412/461 of P76037
- Y110 (= Y115) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
27% identity, 81% coverage: 37:418/470 of query aligns to 49:423/531 of Q9QXW9
- Y130 (= Y115) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ V118) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (= F237) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
27% identity, 81% coverage: 37:418/470 of query aligns to 50:424/535 of Q9UHI5
- I53 (= I40) binding
- Y93 (= Y78) mutation to A: Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.
- N134 (≠ V118) Important for substrate specificity; binding ; mutation to Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; mutation to S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- C154 (≠ A146) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ G167) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F237) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ Y240) Important for substrate specificity; binding ; mutation to S: Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.
- V302 (≠ E295) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ A391) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ A392) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ A397) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R412) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 460 V → E: found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
27% identity, 81% coverage: 37:418/470 of query aligns to 10:384/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
27% identity, 81% coverage: 37:418/470 of query aligns to 10:384/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
27% identity, 81% coverage: 37:418/470 of query aligns to 10:384/458 of 7cmhB
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
24% identity, 88% coverage: 7:418/470 of query aligns to 7:411/487 of P82251
- V40 (= V37) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IVGTG 40:44) binding
- I44 (≠ V41) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (vs. gap) to F: in CSNU; uncertain significance
- P52 (vs. gap) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ V65) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y94) to H: in CSNU; uncertain significance
- G105 (= G100) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W109) to R: in CSNU; uncertain significance
- I120 (≠ E114) to L: in CSNU; uncertain significance
- T123 (≠ L117) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ A136) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ T138) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ L169) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A181) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ V193) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ F237) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A238) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (vs. gap) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (vs. gap) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F242) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A244) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S266) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ I268) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S293) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ L329) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q332) to E: in CSNU; uncertain significance
- V330 (≠ T338) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M339) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R341) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (≠ I361) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T389) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A392) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (vs. gap) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ T394) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P408) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 426 L → P: in CSNU; uncertain significance
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
22% identity, 76% coverage: 12:370/470 of query aligns to 4:356/489 of P25737
- Y102 (≠ L111) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y115) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K187) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F237) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D243) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E251) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
24% identity, 82% coverage: 33:418/470 of query aligns to 7:382/458 of 6li9B
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
23% identity, 85% coverage: 66:463/470 of query aligns to 85:475/501 of Q9UPY5
- C86 (≠ A67) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (≠ Y115) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ T138) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ N180) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V186) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (= K187) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (= Y240) binding
- F254 (≠ T247) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ V264) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ T323) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (= F330) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
- R396 (≠ A392) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
- C414 (≠ A407) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C435 (= C430) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
23% identity, 85% coverage: 66:463/470 of query aligns to 41:431/453 of 7epzB
Sites not aligning to the query:
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
23% identity, 35% coverage: 210:375/470 of query aligns to 172:336/439 of P0AAF1
- W201 (≠ F237) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (≠ D243) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ S246) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ L321) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ P322) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (≠ F328) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ F337) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ M344) mutation to L: Excretion activity decreases more than uptake activity.
Sites not aligning to the query:
- 62 mutation C->A,T: Strong decrease in both uptake and excretion activities.; C→S: Moderate decrease in both uptake and excretion activities.
- 68 K→A: Slight decrease in both uptake and excretion activities.
- 77 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- 78 Y→L: Uptake activity decreases more than excretion activity.
- 82 K→A: Slight decrease in both uptake and excretion activities.
- 90 Y→L: Uptake activity decreases more than excretion activity.
- 92 Y→L: Moderate decrease in both uptake and excretion activities.
- 422 W→L: Uptake activity decreases more than excretion activity.
- 425 Y→F: Moderate decrease in both uptake and excretion activities.; Y→L: Strong decrease in both uptake and excretion activities.
- 433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
23% identity, 85% coverage: 66:463/470 of query aligns to 41:431/455 of 7p9uB
Query Sequence
>Ga0059261_1577 FitnessBrowser__Korea:Ga0059261_1577
MAGGLFRTKRVKDAAEQAPEHRLAATLSWPHLVALGVGAIVGTGILTLIGVGAGKAGPAV
IMSFVIAGAICACAALAYAEMATMMPASGSAYAYSYAVLGEIIAWVVGWSLILEYSLVVS
TVAVGWSGYAAPLLHAWTGMPLELMAGPHANGIVNLPAIFIIAVVAGLLCLGTKESATLN
AALVVVKIIALAVFVAVALPYFNGANLEPFAPFGFAKTISPDGVERGVMAAAAIIFFAFY
GFDAISTAAEETKNPGRDLAIGIVGSMIACVAIYMLVAVAAVGATPFTHFANSPEPLALI
LRDLGRPGFATFLAVSAIIALPTVLLGFLFGQSRIFFTMARDGMLPIGLAKVSKRGSPVR
ITLFTAAIVAVIAGLLPIDEIAALANAGTLAAFTAVAVCMMVLRVRAPDMPRMFRTPLWW
LVGAIAVLGCIYLFFSLPVKTQLWFLAWNALGVVIYFAYARPRVSAKGIE
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory