SitesBLAST
Comparing WP_011814480.1 NCBI__GCF_000015585.1:WP_011814480.1 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)
41% identity, 98% coverage: 7:330/331 of query aligns to 30:352/486 of 4pcuA
- active site: K77 (= K52), S105 (≠ A80), D237 (= D213), S305 (= S283)
- binding protoporphyrin ix containing fe: A182 (≠ T158), P185 (≠ R161), L186 (= L162), Y189 (= Y165), R222 (= R198), T269 (≠ A247)
- binding pyridoxal-5'-phosphate: K77 (= K52), N107 (= N82), G212 (= G188), T213 (= T189), G214 (= G190), T216 (= T192), G261 (= G239), S305 (= S283), P331 (≠ C309), D332 (= D310)
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
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
41% identity, 98% coverage: 7:330/331 of query aligns to 32:356/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ T158), P189 (≠ R161), L190 (= L162), Y193 (= Y165), R226 (= R198)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K52), T106 (= T79), S107 (≠ A80), N109 (= N82), T110 (= T83), Q182 (= Q154), G216 (= G188), T217 (= T189), G218 (= G190), T220 (= T192), G265 (= G239), S309 (= S283), P335 (≠ C309), D336 (= D310)
Sites not aligning to the query:
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
41% identity, 98% coverage: 7:330/331 of query aligns to 31:355/507 of 8s5hA
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)
41% identity, 98% coverage: 7:330/331 of query aligns to 72:396/551 of P35520
- P78 (≠ D13) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- G85 (= G20) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T22) 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 (≠ A42) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P47) 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 (= K52) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ A58) 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 (≠ I59) to V: in CBSD; loss of activity
- E131 (= E64) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G72) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V76) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E77) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G81) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N82) binding pyridoxal 5'-phosphate
- L154 (= L87) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A88) 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 (= C98) 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 (≠ Q106) 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 (= E109) 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 (≠ L113) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (≠ V124) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ A143) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ T158) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N160) 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 (≠ G163) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ R166) 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 188:192) binding pyridoxal 5'-phosphate
- T257 (= T189) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ A194) 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 (= R198) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K201) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ S204) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ T207) 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 (≠ Y210) 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 (= D213) to N: in CBSD; loss of activity
- A288 (≠ G226) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (vs. gap) 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 (= G239) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G241) 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 (≠ I254) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D255) to V: in CBSD; loss of activity
- R336 (≠ Y270) 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 (= L272) 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 (= G281) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S283) 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 (≠ N287) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ T303) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D310) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ G313) 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 (≠ R318) 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
- 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)
40% identity, 98% coverage: 7:330/331 of query aligns to 30:347/348 of 1jbqA
- active site: K77 (= K52), S105 (≠ A80), D232 (= D213), S236 (= S217), L238 (= L219), S300 (= S283), P326 (≠ C309)
- binding protoporphyrin ix containing fe: A177 (≠ T158), P180 (≠ R161), L181 (= L162), Y184 (= Y165), R217 (= R198)
- binding pyridoxal-5'-phosphate: K77 (= K52), N107 (= N82), V206 (≠ T187), G207 (= G188), T208 (= T189), G209 (= G190), G210 (= G191), T211 (= T192), G256 (= G239), S300 (= S283), P326 (≠ C309), D327 (= D310)
Sites not aligning to the query:
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
42% identity, 97% coverage: 9:330/331 of query aligns to 1:316/464 of P9WP51
Sites not aligning to the query:
- 428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
41% identity, 97% coverage: 11:331/331 of query aligns to 8:330/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K52), T82 (= T83), Q154 (= Q154), G188 (= G188), T189 (= T189), G190 (= G190), T192 (= T192), G238 (= G239), I239 (= I240), Y241 (≠ S242), S282 (= S283), P308 (≠ C309), D309 (= D310)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
43% identity, 94% coverage: 19:330/331 of query aligns to 9:314/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
43% identity, 94% coverage: 19:330/331 of query aligns to 9:314/458 of 7xnzB
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
41% identity, 97% coverage: 11:331/331 of query aligns to 8:330/477 of 6xwlC
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
40% identity, 97% coverage: 10:330/331 of query aligns to 34:354/504 of Q2V0C9
- K78 (= K52) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N82) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (= GTGGT 188:192) binding pyridoxal 5'-phosphate
- S307 (= S283) binding pyridoxal 5'-phosphate
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)
40% identity, 97% coverage: 10:330/331 of query aligns to 30:347/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ T158), P184 (≠ R161), Y188 (= Y165), R221 (= R198)
- binding pyridoxal-5'-phosphate: K74 (= K52), N104 (= N82), G209 (≠ A186), G211 (= G188), T212 (= T189), G213 (= G190), G214 (= G191), T215 (= T192), G256 (= G239), S300 (= S283), P326 (≠ C309), D327 (= D310)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
39% identity, 97% coverage: 10:330/331 of query aligns to 38:359/504 of 3pc4A
- active site: K82 (= K52), S312 (= S283)
- binding protoporphyrin ix containing fe: A189 (≠ T158), P192 (≠ R161), L193 (= L162), Y196 (= Y165), R229 (= R198), T276 (≠ A247)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K52), T109 (= T79), S110 (≠ A80), N112 (= N82), T113 (= T83), Q185 (= Q154), A218 (≠ T187), G219 (= G188), T220 (= T189), A221 (≠ G190), T223 (= T192), G268 (= G239), I269 (= I240), Y271 (≠ S242), S312 (= S283), P338 (≠ C309), D339 (= D310)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
39% identity, 97% coverage: 10:330/331 of query aligns to 38:359/504 of 3pc3A
- active site: K82 (= K52), S312 (= S283)
- binding protoporphyrin ix containing fe: A189 (≠ T158), P192 (≠ R161), L193 (= L162), Y196 (= Y165), R229 (= R198)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K52), T109 (= T79), S110 (≠ A80), N112 (= N82), T113 (= T83), Q185 (= Q154), A218 (≠ T187), G219 (= G188), T220 (= T189), A221 (≠ G190), T223 (= T192), G268 (= G239), I269 (= I240), S312 (= S283), P338 (≠ C309), D339 (= D310)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
39% identity, 97% coverage: 10:330/331 of query aligns to 36:357/500 of 3pc2A
- active site: K80 (= K52), S310 (= S283)
- binding protoporphyrin ix containing fe: A187 (≠ T158), P190 (≠ R161), L191 (= L162), Y194 (= Y165), R227 (= R198)
- binding pyridoxal-5'-phosphate: K80 (= K52), N110 (= N82), A216 (≠ T187), G217 (= G188), T218 (= T189), A219 (≠ G190), T221 (= T192), G266 (= G239), S310 (= S283), P336 (≠ C309), D337 (= D310)
Sites not aligning to the query:
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
42% identity, 91% coverage: 17:317/331 of query aligns to 5:297/302 of 2efyA
- active site: K40 (= K52), S70 (≠ A80), E200 (≠ D213), S204 (= S217), S263 (= S283)
- binding 5-oxohexanoic acid: T69 (= T79), G71 (= G81), T73 (= T83), Q141 (= Q154), G175 (= G188), G219 (= G239), M220 (≠ I240), P222 (≠ S242)
- binding pyridoxal-5'-phosphate: K40 (= K52), N72 (= N82), Y172 (≠ A185), G175 (= G188), T176 (= T189), G177 (= G190), T179 (= T192), G219 (= G239), S263 (= S283), P289 (≠ C309), D290 (= D310)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
42% identity, 91% coverage: 17:317/331 of query aligns to 5:297/302 of 2ecqA
- active site: K40 (= K52), S70 (≠ A80), E200 (≠ D213), S204 (= S217), S263 (= S283)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K52), G71 (= G81), T73 (= T83), Q141 (= Q154), G219 (= G239)
- binding pyridoxal-5'-phosphate: K40 (= K52), N72 (= N82), Y172 (≠ A185), G173 (≠ A186), G175 (= G188), T176 (= T189), T179 (= T192), G219 (= G239), S263 (= S283), P289 (≠ C309)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
42% identity, 91% coverage: 17:317/331 of query aligns to 5:297/302 of 2ecoA
- active site: K40 (= K52), S70 (≠ A80), E200 (≠ D213), S204 (= S217), S263 (= S283)
- binding 4-methyl valeric acid: K40 (= K52), T69 (= T79), G71 (= G81), T73 (= T83), Q141 (= Q154), G175 (= G188), T176 (= T189), G219 (= G239)
- binding pyridoxal-5'-phosphate: K40 (= K52), N72 (= N82), Y172 (≠ A185), G175 (= G188), T176 (= T189), T179 (= T192), G219 (= G239), S263 (= S283), P289 (≠ C309), D290 (= D310)
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)
40% identity, 93% coverage: 9:317/331 of query aligns to 1:301/310 of P9WP55
- K44 (= K52) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N82) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (= GTGGT 188:192) binding pyridoxal 5'-phosphate
- S266 (= S283) binding pyridoxal 5'-phosphate
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)
40% identity, 93% coverage: 9:317/331 of query aligns to 1:301/306 of 2q3dA
- active site: K44 (= K52), S266 (= S283), P293 (≠ C309)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K52), T71 (= T79), S72 (≠ A80), N74 (= N82), T75 (= T83), Q144 (= Q154), V177 (≠ T187), G178 (= G188), T179 (= T189), G180 (= G190), T182 (= T192), G222 (= G239), I223 (= I240), S266 (= S283), P293 (≠ C309), D294 (= D310)
Query Sequence
>WP_011814480.1 NCBI__GCF_000015585.1:WP_011814480.1
MSSKRESSMSICDGFVGAIGNTPLIRLPRLSEETGCEILGKAEFMNPGGSVKDRAALAIV
QAAERSGELRPGGTVVEGTAGNTGIGLAHICNARGYRCVIVIPETQSQEKIDLLRTLGAE
VHAVPAAPYRDPGNYQKVAGRMAAEMDNAVWANQFDNTANRLGHYRTTGPEVWAQTGGRV
DAFVAATGTGGTLAGVSRALKERSPDTRIYLADPSGSALYNFVRDGEPAPTAGNSITEGI
GSSRVTANLQGTDIDDAFCISDAESVPMVYRLLREEGLFLGSSSGVNVCGAVRAAEELGP
GHTVVTILCDGGGRYYSRLFNEAWLAERGLA
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