SitesBLAST
Comparing WP_043743637.1 NCBI__GCF_000009985.1:WP_043743637.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
40% identity, 97% coverage: 8:332/334 of query aligns to 38:363/486 of 4pcuA
- active site: K77 (= K45), S105 (≠ A73), D237 (= D211), S305 (= S280)
- binding protoporphyrin ix containing fe: A182 (≠ T156), P185 (≠ R159), L186 (≠ M160), Y189 (≠ F163), R222 (≠ M196), T269 (≠ R244)
- binding pyridoxal-5'-phosphate: K77 (= K45), N107 (= N75), G212 (= G186), T213 (= T187), G214 (= G188), T216 (= T190), G261 (= G236), S305 (= S280), P331 (≠ C306), D332 (= D307)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- 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)
40% identity, 97% coverage: 8:332/334 of query aligns to 80:409/551 of P35520
- G85 (= G13) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T15) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (vs. gap) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (vs. gap) 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 (≠ A35) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P40) 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 (= K45) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ A51) 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 (≠ I52) to V: in CBSD; loss of activity
- E131 (= E57) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G65) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V69) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E70) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G74) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N75) binding
- L154 (= L80) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A81) 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 (≠ T91) 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 (≠ Q99) 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 (= E102) 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 (≠ M106) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V117) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A136) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ T156) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N158) 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 (≠ G161) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ N164) 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 (= GTGGT 186:190) binding
- T257 (= T187) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ A192) 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 (≠ M196) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K199) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ N202) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ I205) 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 (≠ V208) 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 (= D211) to N: in CBSD; loss of activity
- A288 (≠ Y218) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ I233) 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 (= G236) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G238) 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 (≠ I251) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D252) to V: in CBSD; loss of activity
- R336 (≠ F267) 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 (= L269) 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 (= G278) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S280) 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 (≠ N284) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T300) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D307) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ T310) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
- K384 (= K315) to E: in CBSD; severe form; dbSNP:rs121964967
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
- 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
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
40% identity, 97% coverage: 8:332/334 of query aligns to 40:369/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ T156), P189 (≠ R159), L190 (≠ M160), Y193 (≠ F163), R226 (≠ M196)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K45), T106 (= T72), S107 (≠ A73), N109 (= N75), T110 (= T76), Q182 (= Q152), G216 (= G186), T217 (= T187), G218 (= G188), T220 (= T190), G265 (= G236), S309 (= S280), P335 (≠ C306), D336 (= D307)
Sites not aligning to the query:
7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
40% identity, 97% coverage: 8:332/334 of query aligns to 40:369/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ T156), P189 (≠ R159), L190 (≠ M160), Y193 (≠ F163), R226 (≠ M196)
- binding pyridoxal-5'-phosphate: K79 (= K45), N109 (= N75), G216 (= G186), T217 (= T187), G218 (= G188), T220 (= T190), G265 (= G236), S309 (= S280), P335 (≠ C306), D336 (= D307)
Sites not aligning to the query:
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
40% identity, 96% coverage: 4:324/334 of query aligns to 8:326/477 of 6xwlC
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
40% identity, 96% coverage: 4:324/334 of query aligns to 8:326/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K45), T82 (= T76), Q154 (= Q152), G188 (= G186), T189 (= T187), G190 (= G188), T192 (= T190), G238 (= G236), I239 (= I237), Y241 (≠ Q239), S282 (= S280), P308 (≠ C306), D309 (= D307)
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
40% identity, 99% coverage: 2:330/334 of query aligns to 33:357/504 of Q2V0C9
- K78 (= K45) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N75) binding
- GTGGT 215:219 (= GTGGT 186:190) binding
- S307 (= S280) binding
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
41% identity, 99% coverage: 2:330/334 of query aligns to 29:350/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ T156), P184 (≠ R159), Y188 (≠ F163), R221 (≠ M196)
- binding pyridoxal-5'-phosphate: K74 (= K45), N104 (= N75), G209 (≠ A184), G211 (= G186), T212 (= T187), G213 (= G188), G214 (= G189), T215 (= T190), G256 (= G236), S300 (= S280), P326 (≠ C306), D327 (= D307)
Sites not aligning to the query:
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
40% identity, 94% coverage: 12:325/334 of query aligns to 9:318/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
40% identity, 94% coverage: 12:325/334 of query aligns to 9:318/458 of 7xnzB
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 94% coverage: 12:325/334 of query aligns to 11:320/464 of P9WP51
Sites not aligning to the query:
- 428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
42% identity, 91% coverage: 11:314/334 of query aligns to 6:297/302 of 2efyA
- active site: K40 (= K45), S70 (≠ A73), E200 (≠ D211), S204 (= S215), S263 (= S280)
- binding 5-oxohexanoic acid: T69 (= T72), G71 (= G74), T73 (= T76), Q141 (= Q152), G175 (= G186), G219 (= G236), M220 (≠ I237), P222 (≠ Q239)
- binding pyridoxal-5'-phosphate: K40 (= K45), N72 (= N75), Y172 (≠ C183), G175 (= G186), T176 (= T187), G177 (= G188), T179 (= T190), G219 (= G236), S263 (= S280), P289 (≠ C306), D290 (= D307)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
42% identity, 91% coverage: 11:314/334 of query aligns to 6:297/302 of 2ecqA
- active site: K40 (= K45), S70 (≠ A73), E200 (≠ D211), S204 (= S215), S263 (= S280)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K45), G71 (= G74), T73 (= T76), Q141 (= Q152), G219 (= G236)
- binding pyridoxal-5'-phosphate: K40 (= K45), N72 (= N75), Y172 (≠ C183), G173 (≠ A184), G175 (= G186), T176 (= T187), T179 (= T190), G219 (= G236), S263 (= S280), P289 (≠ C306)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
42% identity, 91% coverage: 11:314/334 of query aligns to 6:297/302 of 2ecoA
- active site: K40 (= K45), S70 (≠ A73), E200 (≠ D211), S204 (= S215), S263 (= S280)
- binding 4-methyl valeric acid: K40 (= K45), T69 (= T72), G71 (= G74), T73 (= T76), Q141 (= Q152), G175 (= G186), T176 (= T187), G219 (= G236)
- binding pyridoxal-5'-phosphate: K40 (= K45), N72 (= N75), Y172 (≠ C183), G175 (= G186), T176 (= T187), T179 (= T190), G219 (= G236), S263 (= S280), P289 (≠ C306), D290 (= D307)
P9WP55 O-acetylserine sulfhydrylase; OAS sulfhydrylase; OASS; Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine-specific cysteine synthase; Sulfide-dependent cysteine synthase; EC 2.5.1.47 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 91% coverage: 12:314/334 of query aligns to 11:301/310 of P9WP55
- K44 (= K45) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N75) binding
- GTGGT 178:182 (= GTGGT 186:190) binding
- S266 (= S280) binding
2q3dA 2.2 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) from mycobacterium tuberculosis in complex with the reaction intermediate alpha-aminoacrylate (see paper)
41% identity, 91% coverage: 12:314/334 of query aligns to 11:301/306 of 2q3dA
- active site: K44 (= K45), S266 (= S280), P293 (≠ C306)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K45), T71 (= T72), S72 (≠ A73), N74 (= N75), T75 (= T76), Q144 (= Q152), V177 (= V185), G178 (= G186), T179 (= T187), G180 (= G188), T182 (= T190), G222 (= G236), I223 (= I237), S266 (= S280), P293 (≠ C306), D294 (= D307)
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
41% identity, 90% coverage: 12:312/334 of query aligns to 11:299/300 of 3zeiA
- active site: K44 (= K45), S266 (= S280), P293 (≠ C306)
- binding 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid: T71 (= T72), S72 (≠ A73), I126 (≠ E133), Q144 (= Q152), F145 (= F153), K215 (≠ E229), G222 (= G236), A225 (≠ Q239), F227 (≠ R241)
- binding pyridoxal-5'-phosphate: K44 (= K45), N74 (= N75), V177 (= V185), G178 (= G186), T179 (= T187), G180 (= G188), T182 (= T190), G222 (= G236), S266 (= S280), P293 (≠ C306), D294 (= D307)
2q3cA 2.1 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) holoenzyme from mycobacterium tuberculosis in complex with the inhibitory peptide dfsi (see paper)
41% identity, 90% coverage: 12:312/334 of query aligns to 11:299/300 of 2q3cA
- active site: K44 (= K45), S266 (= S280), P293 (≠ C306)
- binding : T71 (= T72), S72 (≠ A73), G73 (= G74), T75 (= T76), M122 (≠ V129), Q144 (= Q152), K215 (≠ E229), G222 (= G236), A225 (≠ Q239)
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
37% identity, 99% coverage: 4:332/334 of query aligns to 39:369/504 of 3pc4A
- active site: K82 (= K45), S312 (= S280)
- binding protoporphyrin ix containing fe: A189 (≠ T156), P192 (≠ R159), L193 (≠ M160), Y196 (≠ F163), R229 (≠ M196), T276 (≠ R244)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K45), T109 (= T72), S110 (≠ A73), N112 (= N75), T113 (= T76), Q185 (= Q152), A218 (≠ V185), G219 (= G186), T220 (= T187), A221 (≠ G188), T223 (= T190), G268 (= G236), I269 (= I237), Y271 (≠ Q239), S312 (= S280), P338 (≠ C306), D339 (= D307)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
37% identity, 99% coverage: 4:332/334 of query aligns to 39:369/504 of 3pc3A
- active site: K82 (= K45), S312 (= S280)
- binding protoporphyrin ix containing fe: A189 (≠ T156), P192 (≠ R159), L193 (≠ M160), Y196 (≠ F163), R229 (≠ M196)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K45), T109 (= T72), S110 (≠ A73), N112 (= N75), T113 (= T76), Q185 (= Q152), A218 (≠ V185), G219 (= G186), T220 (= T187), A221 (≠ G188), T223 (= T190), G268 (= G236), I269 (= I237), S312 (= S280), P338 (≠ C306), D339 (= D307)
Sites not aligning to the query:
Query Sequence
>WP_043743637.1 NCBI__GCF_000009985.1:WP_043743637.1
MTDIRDGFLDSIGNTPLIRLKRASEETGCNILGKAEFLNPGGSVKDRAALAIIQDAERKG
LLKPGGVIVEGTAGNTGIGLALVANALGYRTVIVMPETQSQEKKDMLRLVGADLRLVPAV
PYANPGNYVRYSETLANELAKTEPNGVLWANQFDNTANRMGHFNTTGQEIWRQTDGTVDA
FTCAVGTGGTLAGTGMALKEHNKDIKVVLADPMGSALYHHYAHGELKAEGTSITEGIGQG
RITRNLDGAPIDDQVQVTDHEALPLIFDLVRQEGLVLGGSSGINVMAAIKVARILGPGHT
VVTVLCDYGTRYQSKLFNPAFLRERNLPVPHWLE
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