SitesBLAST
Comparing WP_012589541.1 NCBI__GCF_000021745.1:WP_012589541.1 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)
39% identity, 97% coverage: 6:337/343 of query aligns to 37:369/486 of 4pcuA
- active site: K77 (= K44), S105 (≠ A72), D237 (= D210), S305 (= S279)
- binding protoporphyrin ix containing fe: A182 (≠ V155), P185 (≠ R158), L186 (≠ Q159), Y189 (≠ F162), R222 (≠ M195), T269 (≠ A243)
- binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), G212 (= G185), T213 (= T186), G214 (= G187), T216 (= T189), G261 (= G235), S305 (= S279), P331 (≠ C305), D332 (= D306)
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
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
38% identity, 97% coverage: 6:337/343 of query aligns to 38:374/507 of 8s5hA
Sites not aligning to the query:
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
38% identity, 97% coverage: 6:337/343 of query aligns to 39:375/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ V155), P189 (≠ R158), L190 (≠ Q159), Y193 (≠ F162), R226 (≠ M195)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K44), T106 (= T71), S107 (≠ A72), N109 (= N74), T110 (= T75), Q182 (= Q151), G216 (= G185), T217 (= T186), G218 (= G187), T220 (= T189), G265 (= G235), S309 (= S279), P335 (≠ C305), D336 (= D306)
Sites not aligning to the query:
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
38% identity, 97% coverage: 7:337/343 of query aligns to 80:415/551 of P35520
- G85 (= G12) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T14) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (≠ T26) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (≠ Q27) 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 (≠ A34) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P39) 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 (= K44) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ A50) 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 (≠ I51) to V: in CBSD; loss of activity
- E131 (≠ V56) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G64) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V68) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E69) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G73) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N74) binding pyridoxal 5'-phosphate
- L154 (= L79) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A80) 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 (≠ T90) 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 (≠ Q98) 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 (= E101) 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 (≠ L105) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V116) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A139) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ V155) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N157) 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 (≠ G160) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ E163) 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 185:189) binding pyridoxal 5'-phosphate
- T257 (= T186) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ A191) 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 (≠ M195) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K198) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ N201) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V204) 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 (≠ A207) 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 (= D210) to N: in CBSD; loss of activity
- A288 (≠ Y217) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ S231) 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 (= G235) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G237) 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 (≠ I250) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D251) to V: in CBSD; loss of activity
- R336 (≠ F266) 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 (= L268) 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 (= G277) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S279) binding pyridoxal 5'-phosphate; 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 (≠ N283) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T299) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D306) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ S309) 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 (= K314) 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
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
39% identity, 93% coverage: 6:324/343 of query aligns to 37:345/348 of 1jbqA
- active site: K77 (= K44), S105 (≠ A72), D232 (= D210), S236 (≠ A214), L238 (= L216), S300 (= S279), P326 (≠ C305)
- binding protoporphyrin ix containing fe: A177 (≠ V155), P180 (≠ R158), L181 (≠ Q159), Y184 (≠ F162), R217 (≠ M195)
- binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), V206 (= V184), G207 (= G185), T208 (= T186), G209 (= G187), G210 (= G188), T211 (= T189), G256 (= G235), S300 (= S279), P326 (≠ C305), D327 (= D306)
Sites not aligning to the query:
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
38% identity, 92% coverage: 6:321/343 of query aligns to 11:324/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K44), T82 (= T75), Q154 (= Q151), G188 (= G185), T189 (= T186), G190 (= G187), T192 (= T189), G238 (= G235), I239 (= I236), Y241 (≠ Q238), S282 (= S279), P308 (≠ C305), D309 (= D306)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
38% identity, 92% coverage: 6:321/343 of query aligns to 11:324/477 of 6xwlC
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 94% coverage: 1:323/343 of query aligns to 1:313/464 of P9WP51
Sites not aligning to the query:
- 428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
41% identity, 94% coverage: 3:323/343 of query aligns to 1:311/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
41% identity, 94% coverage: 3:323/343 of query aligns to 1:311/458 of 7xnzB
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
41% identity, 89% coverage: 10:313/343 of query aligns to 6:297/302 of 2efyA
- active site: K40 (= K44), S70 (≠ A72), E200 (≠ D210), S204 (≠ Y217), S263 (= S279)
- binding 5-oxohexanoic acid: T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q151), G175 (= G185), G219 (= G235), M220 (≠ I236), P222 (≠ Q238)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ S182), G175 (= G185), T176 (= T186), G177 (= G187), T179 (= T189), G219 (= G235), S263 (= S279), P289 (≠ C305), D290 (= D306)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
41% identity, 89% coverage: 10:313/343 of query aligns to 6:297/302 of 2ecqA
- active site: K40 (= K44), S70 (≠ A72), E200 (≠ D210), S204 (≠ Y217), S263 (= S279)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K44), G71 (= G73), T73 (= T75), Q141 (= Q151), G219 (= G235)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ S182), G173 (≠ A183), G175 (= G185), T176 (= T186), T179 (= T189), G219 (= G235), S263 (= S279), P289 (≠ C305)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
41% identity, 89% coverage: 10:313/343 of query aligns to 6:297/302 of 2ecoA
- active site: K40 (= K44), S70 (≠ A72), E200 (≠ D210), S204 (≠ Y217), S263 (= S279)
- binding 4-methyl valeric acid: K40 (= K44), T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q151), G175 (= G185), T176 (= T186), G219 (= G235)
- binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ S182), G175 (= G185), T176 (= T186), T179 (= T189), G219 (= G235), S263 (= S279), P289 (≠ C305), D290 (= D306)
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
38% identity, 94% coverage: 6:329/343 of query aligns to 42:362/504 of 3pc4A
- active site: K82 (= K44), S312 (= S279)
- binding protoporphyrin ix containing fe: A189 (≠ V155), P192 (≠ R158), L193 (≠ Q159), Y196 (≠ F162), R229 (≠ M195), T276 (≠ A243)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K44), T109 (= T71), S110 (≠ A72), N112 (= N74), T113 (= T75), Q185 (= Q151), A218 (≠ V184), G219 (= G185), T220 (= T186), A221 (≠ G187), T223 (= T189), G268 (= G235), I269 (= I236), Y271 (≠ Q238), S312 (= S279), P338 (≠ C305), D339 (= D306)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
38% identity, 94% coverage: 6:329/343 of query aligns to 42:362/504 of 3pc3A
- active site: K82 (= K44), S312 (= S279)
- binding protoporphyrin ix containing fe: A189 (≠ V155), P192 (≠ R158), L193 (≠ Q159), Y196 (≠ F162), R229 (≠ M195)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K44), T109 (= T71), S110 (≠ A72), N112 (= N74), T113 (= T75), Q185 (= Q151), A218 (≠ V184), G219 (= G185), T220 (= T186), A221 (≠ G187), T223 (= T189), G268 (= G235), I269 (= I236), S312 (= S279), P338 (≠ C305), D339 (= D306)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
38% identity, 94% coverage: 6:329/343 of query aligns to 40:360/500 of 3pc2A
- active site: K80 (= K44), S310 (= S279)
- binding protoporphyrin ix containing fe: A187 (≠ V155), P190 (≠ R158), L191 (≠ Q159), Y194 (≠ F162), R227 (≠ M195)
- binding pyridoxal-5'-phosphate: K80 (= K44), N110 (= N74), A216 (≠ V184), G217 (= G185), T218 (= T186), A219 (≠ G187), T221 (= T189), G266 (= G235), S310 (= S279), P336 (≠ C305), D337 (= D306)
Sites not aligning to the query:
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
36% identity, 94% coverage: 6:326/343 of query aligns to 9:335/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G175), N183 (≠ R176)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K44), N80 (= N74), A191 (≠ V184), G192 (= G185), T193 (= T186), G194 (= G187), T196 (= T189), G241 (= G235), S285 (= S279), P314 (≠ C305), D315 (= D306)
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
36% identity, 94% coverage: 6:326/343 of query aligns to 10:336/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G175), N184 (≠ R176)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K44), T78 (= T71), S79 (≠ A72), N81 (= N74), T82 (= T75), Q154 (= Q151), A192 (≠ V184), G193 (= G185), T194 (= T186), G195 (= G187), T197 (= T189), G242 (= G235), S286 (= S279), P315 (≠ C305), D316 (= D306)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
36% identity, 94% coverage: 6:326/343 of query aligns to 10:336/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G175), N184 (≠ R176)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K44), T78 (= T71), S79 (≠ A72), N81 (= N74), T82 (= T75), Q154 (= Q151), A192 (≠ V184), G193 (= G185), T194 (= T186), G195 (= G187), T197 (= T189), G242 (= G235), Y245 (≠ Q238), S286 (= S279), P315 (≠ C305), D316 (= D306)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
36% identity, 94% coverage: 6:326/343 of query aligns to 10:336/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G175), N184 (≠ R176)
- binding pyridoxal-5'-phosphate: K50 (= K44), N81 (= N74), A192 (≠ V184), G193 (= G185), T194 (= T186), G195 (= G187), T197 (= T189), G242 (= G235), S286 (= S279), P315 (≠ C305), D316 (= D306)
Query Sequence
>WP_012589541.1 NCBI__GCF_000021745.1:WP_012589541.1
MAFAKSVIEAIGNTPLIKLRRASEETQCLILGKAEFQNPGGSVKDRAALAIVADAVARGA
LKPGGVIVEGTAGNTGIGLALVANALGYKTVIVIPETQSQEKKDLLRLQGAELIEVPAVP
YADPNNYVKLSGRLAERLAKENPAGAIWANQFDNVANRQGHFETTGPEIFAQTDGRVDGF
VSAVGTGGTLAGVGMALKAKNPGVQIALADPPGAALYSYYTTGELKSSGSSITEGIGQGR
ITANLEGAPIDFAYQIGDEESVRLVFDLAENEGLLLGGSSGVNVAGAIRLARELGPGHTI
VTILCDSGSRYQSKLFNPEFLRSKNLPTPGWLERPLQIKPDFL
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