SitesBLAST
Comparing Synpcc7942_2612 FitnessBrowser__SynE:Synpcc7942_2612 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)
2zsjA Crystal structure of threonine synthase from aquifex aeolicus vf5
60% identity, 95% coverage: 18:366/366 of query aligns to 2:350/350 of 2zsjA
- active site: K61 (= K77), T85 (= T101), Q218 (= Q234), A222 (≠ S238), A240 (= A256), T317 (= T331)
- binding pyridoxal-5'-phosphate: F60 (= F76), K61 (= K77), N87 (= N103), V186 (≠ M202), G187 (= G203), N188 (= N204), A189 (= A205), G190 (= G206), N191 (= N207), A240 (= A256), T317 (= T331), G318 (= G332)
6nmxA Threonine synthase from bacillus subtilis atcc 6633 with plp and appa (see paper)
61% identity, 90% coverage: 18:346/366 of query aligns to 3:330/350 of 6nmxA
- active site: K60 (= K77), T84 (= T101), E216 (≠ Q234), S220 (= S238), A238 (= A256), T315 (= T331)
- binding (2E,3Z)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-5-phosphonopent-3-enoic acid: K60 (= K77), S83 (= S100), T84 (= T101), N86 (= N103), T87 (= T104), F133 (= F150), N153 (= N170), S154 (= S171), R159 (= R176), V185 (≠ M202), G186 (= G203), N187 (= N204), A188 (= A205), G189 (= G206), N190 (= N207), A238 (= A256), I239 (= I257), E285 (= E303), T315 (= T331)
6cgqB Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
61% identity, 90% coverage: 18:346/366 of query aligns to 1:328/345 of 6cgqB
- active site: K58 (= K77), T82 (= T101), E214 (≠ Q234), S218 (= S238), A236 (= A256), T313 (= T331)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine: K58 (= K77), S81 (= S100), T82 (= T101), N84 (= N103), T85 (= T104), V183 (≠ M202), G184 (= G203), N185 (= N204), A186 (= A205), N188 (= N207), A236 (= A256), I237 (= I257), E283 (= E303), T313 (= T331)
- binding phosphate ion: K58 (= K77), T85 (= T104), N151 (= N170), S152 (= S171), R157 (= R176), N185 (= N204)
6cgqA Threonine synthase from bacillus subtilis atcc 6633 with plp and plp- ala (see paper)
60% identity, 89% coverage: 20:346/366 of query aligns to 1:320/339 of 6cgqA
- active site: K56 (= K77), T80 (= T101), E206 (≠ Q234), S210 (= S238), A228 (= A256), T305 (= T331)
- binding pyridoxal-5'-phosphate: F55 (= F76), K56 (= K77), N82 (= N103), V175 (≠ M202), G176 (= G203), N177 (= N204), A178 (= A205), G179 (= G206), N180 (= N207), A228 (= A256), E275 (= E303), T305 (= T331), G306 (= G332)
3aeyA Apo form of threonine synthase from thermus thermophilus hb8 (see paper)
59% identity, 88% coverage: 19:341/366 of query aligns to 2:326/350 of 3aeyA
- active site: K60 (= K77), T84 (= T101), P211 (= P228), G215 (= G232), Q217 (= Q234), A239 (= A256), T316 (= T331)
- binding sulfate ion: K60 (= K77), K60 (= K77), G85 (= G102), N86 (= N103), T87 (= T104), T87 (= T104), S154 (= S171), R159 (= R176), N187 (= N204), R228 (≠ E245), V230 (= V247), E231 (≠ Q248), R232 (≠ S249), A239 (= A256)
3aexA Catalytic intermediate analogue of threonine synthase from thermus thermophilus hb8 (see paper)
59% identity, 88% coverage: 19:341/366 of query aligns to 3:327/351 of 3aexA
- active site: K61 (= K77), T85 (= T101), P212 (= P228), G216 (= G232), Q218 (= Q234), A240 (= A256), T317 (= T331)
- binding (3E)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-oxobut-3-enoic acid: K61 (= K77), S84 (= S100), T85 (= T101), N87 (= N103), T88 (= T104), V186 (≠ M202), G187 (= G203), N188 (= N204), A189 (= A205), G190 (= G206), N191 (= N207), A240 (= A256), I241 (= I257), E287 (= E303), T317 (= T331)
- binding phosphate ion: K61 (= K77), T88 (= T104), N154 (= N170), S155 (= S171), R160 (= R176), N188 (= N204)
1v7cA Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue (see paper)
59% identity, 88% coverage: 19:341/366 of query aligns to 3:327/351 of 1v7cA
- active site: K61 (= K77), T85 (= T101), P212 (= P228), G216 (= G232), Q218 (= Q234), A240 (= A256), T317 (= T331)
- binding (2e)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-5-phosphonopent-2-enoic acid: K61 (= K77), S84 (= S100), T85 (= T101), N87 (= N103), T88 (= T104), F134 (= F150), N154 (= N170), S155 (= S171), R160 (= R176), V186 (≠ M202), G187 (= G203), N188 (= N204), A189 (= A205), G190 (= G206), N191 (= N207), A240 (= A256), I241 (= I257), E287 (= E303), T317 (= T331)
1uimA Crystal structure of threonine synthase from thermus thermophilus hb8, orthorhombic crystal form (see paper)
59% identity, 88% coverage: 19:341/366 of query aligns to 3:327/350 of 1uimA
- active site: K61 (= K77), T85 (= T101), P212 (= P228), G216 (= G232), Q218 (= Q234), A240 (= A256), T317 (= T331)
- binding pyridoxal-5'-phosphate: F60 (= F76), K61 (= K77), N87 (= N103), G187 (= G203), N188 (= N204), A189 (= A205), G190 (= G206), N191 (= N207), A240 (= A256), E287 (= E303), T317 (= T331), G318 (= G332)
A0R220 Threonine synthase; TS; EC 4.2.3.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
58% identity, 89% coverage: 18:343/366 of query aligns to 12:338/360 of A0R220
- K151 (≠ E159) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P9WG59 Threonine synthase; TS; EC 4.2.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
58% identity, 91% coverage: 11:343/366 of query aligns to 5:338/360 of P9WG59
- K69 (= K77) modified: N6-(pyridoxal phosphate)lysine
- N95 (= N103) binding
- K151 (≠ E159) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- GNAGN 196:200 (= GNAGN 203:207) binding
- T326 (= T331) binding
2d1fA Structure of mycobacterium tuberculosis threonine synthase (see paper)
59% identity, 89% coverage: 18:343/366 of query aligns to 3:329/349 of 2d1fA
- active site: K60 (= K77), T84 (= T101), D209 (≠ Q225), R213 (= R229), L215 (≠ M231), A240 (= A256), T317 (= T331)
- binding pyridoxal-5'-phosphate: F59 (= F76), K60 (= K77), N86 (= N103), V186 (≠ M202), G187 (= G203), N188 (= N204), A189 (= A205), G190 (= G206), N191 (= N207), A240 (= A256), T317 (= T331)
2c2bA Crystallographic structure of arabidopsis thaliana threonine synthase complexed with pyridoxal phosphate and s-adenosylmethionine (see paper)
34% identity, 89% coverage: 18:344/366 of query aligns to 66:410/444 of 2c2bA
- binding pyridoxal-5'-phosphate: F127 (= F76), K128 (= K77), D159 (≠ N103), G259 (≠ M202), G260 (= G203), N261 (= N204), L262 (≠ A205), G263 (= G206), N264 (= N207), A321 (= A256), H369 (≠ A305), T397 (= T331)
- binding s-adenosylmethionine: W66 (= W18), P67 (= P19), G69 (vs. gap), S90 (≠ T39), F92 (≠ H41), N97 (≠ P46), L98 (= L47), W100 (≠ P49), W115 (≠ F64), W115 (≠ F64), Q246 (≠ V190), F247 (≠ L191)
Sites not aligning to the query:
Q9S7B5 Threonine synthase 1, chloroplastic; Protein METHIONINE OVER-ACCUMULATOR 2; EC 4.2.3.1 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
34% identity, 89% coverage: 18:344/366 of query aligns to 141:485/526 of Q9S7B5
- N172 (≠ P46) binding
- L173 (= L47) binding
- K181 (≠ R55) binding in monomer B; binding in monomer A
- N187 (≠ V61) binding in monomer B
- L205 (≠ R79) mutation to R: In mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine.
2c2gA Crystal structure of threonine synthase from arabidopsis thaliana in complex with its cofactor pyridoxal phosphate (see paper)
33% identity, 89% coverage: 18:344/366 of query aligns to 84:412/448 of 2c2gA
P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
28% identity, 85% coverage: 43:352/366 of query aligns to 9:300/303 of P16703
- N71 (= N103) binding
- S255 (≠ A305) binding
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
28% identity, 82% coverage: 43:342/366 of query aligns to 9:291/294 of 2bhtA
- active site: K41 (= K77), S69 (≠ T101), Q199 (≠ V247), G203 (≠ D251), S255 (≠ A305), C280 (≠ T331)
- binding pyridoxal-5'-phosphate: K41 (= K77), N71 (= N103), M173 (= M202), G174 (= G203), T175 (≠ N204), T176 (≠ A205), T178 (≠ N207), G208 (≠ A256), S255 (≠ A305), C280 (≠ T331)
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
26% identity, 79% coverage: 43:330/366 of query aligns to 43:330/486 of 4pcuA
- active site: K77 (= K77), S105 (≠ T101), D237 (≠ Q234), S305 (≠ A305)
- binding protoporphyrin ix containing fe: A182 (≠ S171), P185 (= P174), L186 (= L177), Y189 (≠ Q180), R222 (≠ K221), T269 (≠ A263)
- binding pyridoxal-5'-phosphate: K77 (= K77), N107 (= N103), G212 (= G203), T213 (≠ N204), G214 (≠ A205), T216 (≠ N207), G261 (≠ R258), S305 (≠ A305)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- binding pyridoxal-5'-phosphate: 331, 332
- binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
26% identity, 79% coverage: 43:330/366 of query aligns to 85:374/551 of P35520
- G85 (= G43) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T45) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (≠ R59) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (≠ G60) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
- C109 (≠ Y67) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P72) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
- K119 (= K77) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ M83) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
- M126 (≠ A84) to V: in CBSD; loss of activity
- E131 (≠ K89) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (vs. gap) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (= I97) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (≠ C98) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G102) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N103) binding
- L154 (≠ A108) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A109) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- C165 (≠ A119) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
- M173 (≠ F127) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
- E176 (≠ Q130) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
- V180 (≠ Q135) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ I146) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ V157) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ S171) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N173) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
- A231 (≠ E178) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ K181) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
- GTGGT 256:260 (≠ GNAGN 203:207) binding
- T257 (≠ N204) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ S209) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
- R266 (≠ K221) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (≠ S224) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ L227) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (vs. gap) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
- I278 (≠ M231) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
- D281 (≠ Q234) to N: in CBSD; loss of activity
- A288 (≠ L241) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ T255) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
- G305 (≠ R258) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G260) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
- V320 (≠ S275) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (≠ N276) to V: in CBSD; loss of activity
- R336 (= R292) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
- L338 (= L294) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- G347 (≠ E303) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (≠ A305) binding ; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- T353 (≠ S309) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T325) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
Sites not aligning to the query:
- 18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
- 49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
- 52 binding axial binding residue
- 58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
- 65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
- 69 A → P: in dbSNP:rs17849313
- 78 P → R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- 376 D → N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- 379 R → Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
- 384 K → E: in CBSD; severe form; dbSNP:rs121964967
- 422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- 427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- 435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- 439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- 444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- 449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- 466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- 500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- 526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
- 539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- 540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
A4F2N8 L-threo-3-hydroxyaspartate ammonia-lyase; L-threo-3-hydroxyaspartate dehydratase; L-THA DH; EC 4.3.1.16 from Pseudomonas sp. (see paper)
30% identity, 79% coverage: 45:333/366 of query aligns to 23:307/319 of A4F2N8
- K53 (= K77) mutation to A: Loss of enzymatic activity.
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
26% identity, 79% coverage: 43:330/366 of query aligns to 45:334/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ S171), P189 (= P174), L190 (= L177), Y193 (≠ Q180), R226 (≠ K221)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K77), T106 (≠ S100), S107 (≠ T101), N109 (= N103), T110 (= T104), Q182 (≠ T167), G216 (= G203), T217 (≠ N204), G218 (≠ A205), T220 (≠ N207), G265 (≠ R258), S309 (≠ A305)
Sites not aligning to the query:
Query Sequence
>Synpcc7942_2612 FitnessBrowser__SynE:Synpcc7942_2612
VTATYPSEAQPQSRAHGWPGLIEAYRDYLPVTDTTPIVTLHEGNTPLIPVPTIAREIGRG
VEVFVKYDGLNPTGSFKDRGMTMAITKAKEAGAKAVICASTGNTSAAAAAYARRGGLRAF
VLIPDGFVAQGKLAQALLYGAEVLAIKGNFDRALEIVREVANQYPVTLVNSLNPYRLEGQ
KTAAFELIDVLGEAPDWLCIPMGNAGNISAYWMGFQEYHAKGLSQKLPRMMGFQAAGSAP
LVTGEIVQSPDTIATAIRIGNPANWQRALRVHEESNGAFNAVTDAEILDAYRMLAGQEGI
FCEPASAASVAGMLKCKDEIPDGATIVCVLTGNGLKDPSSAIEFSHTGFKAGIEPDLDIV
AHTMGF
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