SitesBLAST
Comparing WP_012467019.1 NCBI__GCF_000020465.1:WP_012467019.1 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)
7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
35% identity, 97% coverage: 13:456/457 of query aligns to 12:457/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
35% identity, 97% coverage: 13:456/457 of query aligns to 12:457/458 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)
35% identity, 97% coverage: 13:456/457 of query aligns to 14:459/464 of P9WP51
- K428 (≠ D424) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
31% identity, 94% coverage: 5:435/457 of query aligns to 38:471/507 of 8s5hA
Sites not aligning to the query:
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
31% identity, 94% coverage: 5:435/457 of query aligns to 39:472/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P150), P189 (≠ R153), L190 (≠ D154), Y193 (≠ S157), R226 (≠ H190)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (≠ Y43), T106 (= T70), S107 (≠ Y71), N109 (= N73), T110 (≠ S74), Q182 (≠ L146), G216 (≠ I180), T217 (≠ S181), G218 (= G182), T220 (≠ M184), G265 (≠ E230), S309 (≠ A274), P335 (≠ N300), D336 (= D301)
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)
31% identity, 94% coverage: 5:435/457 of query aligns to 79:512/551 of P35520
- G85 (≠ T11) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T13) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (= L25) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (= K26) 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 (≠ L33) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P38) 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 (≠ Y43) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ A49) 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 (≠ V50) to V: in CBSD; loss of activity
- E131 (= E55) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G63) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V67) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (≠ D68) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G72) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N73) binding pyridoxal 5'-phosphate
- L154 (= L78) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A79) 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 (≠ L89) 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 (≠ I97) 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 (= E100) 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 (= V104) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (= T115) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ V135) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ P150) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (≠ S152) 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 (≠ V155) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (≠ N158) 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 (≠ ISGAM 180:184) binding pyridoxal 5'-phosphate
- T257 (≠ S181) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ S186) 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 (≠ H190) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K193) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ K196) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ I199) 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 (= I202) 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 (≠ E205) to N: in CBSD; loss of activity
- A288 (≠ Q212) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (= E227) 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 (≠ E230) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G232) 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 (≠ I245) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D246) to V: in CBSD; loss of activity
- R336 (= R261) 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 (= L263) 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 (= G272) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (≠ A274) 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 (≠ V278) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ C294) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D301) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ G304) 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 (= K309) to E: in CBSD; severe form; dbSNP:rs121964967
- P422 (vs. gap) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- P427 (= P351) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ F359) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (≠ K363) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S368) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (= V373) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ I379) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (= S389) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (= S423) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
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
- 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
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
31% identity, 94% coverage: 5:435/457 of query aligns to 37:466/486 of 4pcuA
- active site: K77 (≠ Y43), S105 (≠ Y71), D237 (≠ E205), S305 (≠ A274)
- binding protoporphyrin ix containing fe: A182 (≠ P150), P185 (≠ R153), L186 (≠ D154), Y189 (≠ S157), R222 (≠ H190), T269 (≠ G238)
- binding pyridoxal-5'-phosphate: K77 (≠ Y43), N107 (= N73), G212 (≠ I180), T213 (≠ S181), G214 (= G182), T216 (≠ M184), G261 (≠ E230), S305 (≠ A274), P331 (≠ N300), D332 (= D301)
- binding s-adenosylmethionine: P376 (≠ D345), G396 (≠ D366), F397 (≠ V367), D398 (≠ S368), Q399 (= Q369)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- binding s-adenosylmethionine: 476, 478, 479
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
32% identity, 86% coverage: 13:407/457 of query aligns to 48:453/500 of 3pc2A
- active site: K80 (≠ Y43), S310 (≠ A274)
- binding protoporphyrin ix containing fe: A187 (≠ P150), P190 (≠ R153), L191 (≠ D154), Y194 (≠ S157), R227 (≠ H190)
- binding pyridoxal-5'-phosphate: K80 (≠ Y43), N110 (= N73), A216 (≠ M179), G217 (≠ I180), T218 (≠ S181), A219 (≠ G182), T221 (≠ M184), G266 (≠ E230), S310 (≠ A274), P336 (≠ N300), D337 (= D301)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
32% identity, 86% coverage: 13:407/457 of query aligns to 50:455/504 of 3pc4A
- active site: K82 (≠ Y43), S312 (≠ A274)
- binding protoporphyrin ix containing fe: A189 (≠ P150), P192 (≠ R153), L193 (≠ D154), Y196 (≠ S157), R229 (≠ H190), T276 (≠ G238)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (≠ Y43), T109 (= T70), S110 (≠ Y71), N112 (= N73), T113 (≠ S74), Q185 (≠ L146), A218 (≠ M179), G219 (≠ I180), T220 (≠ S181), A221 (≠ G182), T223 (≠ M184), G268 (≠ E230), I269 (= I231), Y271 (≠ A233), S312 (≠ A274), P338 (≠ N300), D339 (= D301)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
32% identity, 86% coverage: 13:407/457 of query aligns to 50:455/504 of 3pc3A
- active site: K82 (≠ Y43), S312 (≠ A274)
- binding protoporphyrin ix containing fe: A189 (≠ P150), P192 (≠ R153), L193 (≠ D154), Y196 (≠ S157), R229 (≠ H190)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (≠ Y43), T109 (= T70), S110 (≠ Y71), N112 (= N73), T113 (≠ S74), Q185 (≠ L146), A218 (≠ M179), G219 (≠ I180), T220 (≠ S181), A221 (≠ G182), T223 (≠ M184), G268 (≠ E230), I269 (= I231), S312 (≠ A274), P338 (≠ N300), D339 (= D301)
Sites not aligning to the query:
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
36% identity, 69% coverage: 5:321/457 of query aligns to 37:347/348 of 1jbqA
- active site: K77 (≠ Y43), S105 (≠ Y71), D232 (≠ E205), S236 (= S209), L238 (≠ Y211), S300 (≠ A274), P326 (≠ N300)
- binding protoporphyrin ix containing fe: A177 (≠ P150), P180 (≠ R153), L181 (≠ D154), Y184 (≠ S157), R217 (≠ H190)
- binding pyridoxal-5'-phosphate: K77 (≠ Y43), N107 (= N73), V206 (≠ M179), G207 (≠ I180), T208 (≠ S181), G209 (= G182), G210 (≠ A183), T211 (≠ M184), G256 (≠ E230), S300 (≠ A274), P326 (≠ N300), D327 (= D301)
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
35% identity, 85% coverage: 5:392/457 of query aligns to 38:428/504 of Q2V0C9
- K78 (≠ Y43) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N73) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (≠ ISGAM 180:184) binding pyridoxal 5'-phosphate
- S307 (≠ A274) 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)
35% identity, 85% coverage: 5:392/457 of query aligns to 34:421/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (= P150), P184 (≠ R153), Y188 (≠ S157), R221 (≠ H190)
- binding pyridoxal-5'-phosphate: K74 (≠ Y43), N104 (= N73), G209 (≠ P178), G211 (≠ I180), T212 (≠ S181), G213 (= G182), G214 (≠ A183), T215 (≠ M184), G256 (≠ E230), S300 (≠ A274), P326 (≠ N300), D327 (= D301)
Sites not aligning to the query:
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
32% identity, 85% coverage: 13:402/457 of query aligns to 19:414/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (≠ Y43), T82 (≠ S74), Q154 (≠ L146), G188 (≠ I180), T189 (≠ S181), G190 (= G182), T192 (≠ M184), G238 (≠ E230), I239 (= I231), Y241 (≠ A233), S282 (≠ A274), P308 (≠ N300), D309 (= D301)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
32% identity, 85% coverage: 13:402/457 of query aligns to 19:422/477 of 6xwlC
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
34% identity, 70% coverage: 2:322/457 of query aligns to 7:337/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ S170), N184 (≠ R171)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (≠ Y43), T78 (= T70), S79 (≠ Y71), N81 (= N73), T82 (≠ S74), Q154 (≠ L146), A192 (≠ M179), G193 (≠ I180), T194 (≠ S181), G195 (= G182), T197 (≠ M184), G242 (≠ E230), S286 (≠ A274), P315 (≠ N300), D316 (= D301)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
34% identity, 70% coverage: 2:322/457 of query aligns to 7:337/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ S170), N184 (≠ R171)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (≠ Y43), T78 (= T70), S79 (≠ Y71), N81 (= N73), T82 (≠ S74), Q154 (≠ L146), A192 (≠ M179), G193 (≠ I180), T194 (≠ S181), G195 (= G182), T197 (≠ M184), G242 (≠ E230), Y245 (≠ A233), S286 (≠ A274), P315 (≠ N300), D316 (= D301)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
34% identity, 70% coverage: 2:322/457 of query aligns to 7:337/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ S170), N184 (≠ R171)
- binding pyridoxal-5'-phosphate: K50 (≠ Y43), N81 (= N73), A192 (≠ M179), G193 (≠ I180), T194 (≠ S181), G195 (= G182), T197 (≠ M184), G242 (≠ E230), S286 (≠ A274), P315 (≠ N300), D316 (= D301)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
34% identity, 70% coverage: 2:322/457 of query aligns to 6:336/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ S170), N183 (≠ R171)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (≠ Y43), N80 (= N73), A191 (≠ M179), G192 (≠ I180), T193 (≠ S181), G194 (= G182), T196 (≠ M184), G241 (≠ E230), S285 (≠ A274), P314 (≠ N300), D315 (= D301)
6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
34% identity, 69% coverage: 5:321/457 of query aligns to 6:316/317 of 6vjuB
Query Sequence
>WP_012467019.1 NCBI__GCF_000020465.1:WP_012467019.1
MSNHDIFGISTETPLVYIGQMARYLKAKVMAKLEYMNPACSHYYRAASAVIRDAEERKLI
HPGMTLVDWTYGNSGIALAMAGVSRGYKLLLAAPDKISNEKKDVLKALGAEIVITPSDAL
PEEPRSCMKVAESLVRNIPNAFFANLYENPVSRDVHSNSTGREILQQTESRVTHVFVPMI
SGAMISGIGHLLKAEKPSIRIIGVEPEGSIYQSLFRKGVQDKPAAYELEEIGALQPSGFW
DPSVIDDIVQVSDNDAFNCGRELLRAEAIFAGGASGAVMAAALHSAAAYGENDCIVAVLN
DFGGYYLSKMFRDGWMKQKGYYRKAKTALEQITAEDILQLKARKDLIFANPEATLAEVFE
MMKQNDVSQLPIVSYGTPIGSISENKILSILIENDEAMNSKVVGFMEPPFPVCQTDATIS
ELSDKLQQSASGILISLSDGRLQLLTKSDLIDALTHK
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