SitesBLAST
Comparing WP_010933579.1 NCBI__GCF_000006985.1:WP_010933579.1 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)
P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 100% coverage: 1:454/456 of query aligns to 3:458/464 of P9WP51
- K428 (≠ E423) 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)
34% identity, 100% coverage: 1:454/456 of query aligns to 1:456/458 of 7xoyA
7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
34% identity, 100% coverage: 1:454/456 of query aligns to 1:456/458 of 7xnzB
8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
28% identity, 95% coverage: 4:434/456 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)
28% identity, 95% coverage: 4:434/456 of query aligns to 39:472/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ P149), P189 (≠ R152), L190 (≠ Q153), Y193 (≠ Q156), R226 (= R189)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (≠ Y42), T106 (= T69), S107 (≠ F70), N109 (≠ T72), T110 (≠ S73), Q182 (≠ M145), G216 (≠ A179), T217 (≠ S180), G218 (= G181), T220 (≠ M183), G265 (≠ D229), S309 (≠ A273), P335 (≠ T299), D336 (= D300)
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)
28% identity, 95% coverage: 4:434/456 of query aligns to 79:512/551 of P35520
- G85 (≠ D10) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T12) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (≠ K24) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (≠ R25) 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 (≠ L32) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P37) 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 (≠ Y42) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ A48) 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 (≠ I49) to V: in CBSD; loss of activity
- E131 (= E54) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G62) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (≠ V66) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (≠ D67) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G71) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (≠ T72) binding pyridoxal 5'-phosphate
- L154 (= L77) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (= A78) 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 (≠ V88) 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 (≠ I96) 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 (= E99) 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 (= V103) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (= T114) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ V134) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ P149) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (≠ S151) 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 (≠ V154) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (= D157) 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 (≠ ASGAM 179:183) binding pyridoxal 5'-phosphate
- T257 (≠ S180) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (≠ S185) 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 (= R189) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K192) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ N195) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ V198) 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 (= I201) 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 (≠ E204) to N: in CBSD; loss of activity
- A288 (≠ G211) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ Q226) 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 (≠ D229) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (= G231) 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 (≠ I244) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D245) to V: in CBSD; loss of activity
- R336 (= R260) 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 (= L262) 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 (= G271) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (≠ A273) 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 (≠ A277) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ L293) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D300) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ G303) 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 (≠ R308) 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 (= P350) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- I435 (≠ F358) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- R439 (≠ K362) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- D444 (≠ S367) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- V449 (= V372) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- L456 (≠ I378) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- S466 (= S388) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- S500 (= S422) 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
6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
29% identity, 100% coverage: 1:456/456 of query aligns to 8:467/468 of 6xylA
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (≠ Y42), T82 (≠ S73), Q154 (≠ M145), G188 (≠ A179), T189 (≠ S180), G190 (= G181), T192 (≠ M183), G238 (≠ D229), I239 (= I230), Y241 (≠ A232), S282 (≠ A273), P308 (≠ T299), D309 (= D300)
6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
29% identity, 100% coverage: 1:456/456 of query aligns to 8:476/477 of 6xwlC
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
28% identity, 100% coverage: 1:454/456 of query aligns to 39:496/504 of 3pc4A
- active site: K82 (≠ Y42), S312 (≠ A273)
- binding protoporphyrin ix containing fe: A189 (≠ P149), P192 (≠ R152), L193 (≠ Q153), Y196 (≠ Q156), R229 (= R189), T276 (≠ S237)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (≠ Y42), T109 (= T69), S110 (≠ F70), N112 (≠ T72), T113 (≠ S73), Q185 (≠ M145), A218 (≠ M178), G219 (≠ A179), T220 (≠ S180), A221 (≠ G181), T223 (≠ M183), G268 (≠ D229), I269 (= I230), Y271 (≠ A232), S312 (≠ A273), P338 (≠ T299), D339 (= D300)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
28% identity, 100% coverage: 1:454/456 of query aligns to 39:496/504 of 3pc3A
- active site: K82 (≠ Y42), S312 (≠ A273)
- binding protoporphyrin ix containing fe: A189 (≠ P149), P192 (≠ R152), L193 (≠ Q153), Y196 (≠ Q156), R229 (= R189)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (≠ Y42), T109 (= T69), S110 (≠ F70), N112 (≠ T72), T113 (≠ S73), Q185 (≠ M145), A218 (≠ M178), G219 (≠ A179), T220 (≠ S180), A221 (≠ G181), T223 (≠ M183), G268 (≠ D229), I269 (= I230), S312 (≠ A273), P338 (≠ T299), D339 (= D300)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
28% identity, 100% coverage: 1:454/456 of query aligns to 37:494/500 of 3pc2A
- active site: K80 (≠ Y42), S310 (≠ A273)
- binding protoporphyrin ix containing fe: A187 (≠ P149), P190 (≠ R152), L191 (≠ Q153), Y194 (≠ Q156), R227 (= R189)
- binding pyridoxal-5'-phosphate: K80 (≠ Y42), N110 (≠ T72), A216 (≠ M178), G217 (≠ A179), T218 (≠ S180), A219 (≠ G181), T221 (≠ M183), G266 (≠ D229), S310 (≠ A273), P336 (≠ T299), D337 (= D300)
Sites not aligning to the query:
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
28% identity, 95% coverage: 4:434/456 of query aligns to 37:466/486 of 4pcuA
- active site: K77 (≠ Y42), S105 (≠ F70), D237 (≠ E204), S305 (≠ A273)
- binding protoporphyrin ix containing fe: A182 (≠ P149), P185 (≠ R152), L186 (≠ Q153), Y189 (≠ Q156), R222 (= R189), T269 (≠ S237)
- binding pyridoxal-5'-phosphate: K77 (≠ Y42), N107 (≠ T72), G212 (≠ A179), T213 (≠ S180), G214 (= G181), T216 (≠ M183), G261 (≠ D229), S305 (≠ A273), P331 (≠ T299), D332 (= D300)
- binding s-adenosylmethionine: P376 (≠ L345), G396 (≠ D365), F397 (≠ V366), D398 (≠ S367), Q399 (= Q368)
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
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
29% identity, 99% coverage: 4:455/456 of query aligns to 38:494/504 of Q2V0C9
- K78 (≠ Y42) modified: N6-(pyridoxal phosphate)lysine
- N108 (≠ T72) binding pyridoxal 5'-phosphate
- GTGGT 215:219 (≠ ASGAM 179:183) binding pyridoxal 5'-phosphate
- S307 (≠ A273) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
33% identity, 70% coverage: 4:320/456 of query aligns to 37:347/348 of 1jbqA
- active site: K77 (≠ Y42), S105 (≠ F70), D232 (≠ E204), S236 (= S208), L238 (≠ Y210), S300 (≠ A273), P326 (≠ T299)
- binding protoporphyrin ix containing fe: A177 (≠ P149), P180 (≠ R152), L181 (≠ Q153), Y184 (≠ Q156), R217 (= R189)
- binding pyridoxal-5'-phosphate: K77 (≠ Y42), N107 (≠ T72), V206 (≠ M178), G207 (≠ A179), T208 (≠ S180), G209 (= G181), G210 (≠ A182), T211 (≠ M183), G256 (≠ D229), S300 (≠ A273), P326 (≠ T299), D327 (= D300)
Sites not aligning to the query:
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
29% identity, 99% coverage: 4:455/456 of query aligns to 34:487/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (= P149), P184 (≠ R152), Y188 (≠ Q156), R221 (= R189)
- binding pyridoxal-5'-phosphate: K74 (≠ Y42), N104 (≠ T72), G209 (≠ P177), G211 (≠ A179), T212 (≠ S180), G213 (= G181), G214 (≠ A182), T215 (≠ M183), G256 (≠ D229), S300 (≠ A273), P326 (≠ T299), D327 (= D300)
Sites not aligning to the query:
6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
31% identity, 70% coverage: 3:321/456 of query aligns to 9:337/345 of 6c2zA
- binding calcium ion: N180 (vs. gap), D183 (≠ G169), N184 (≠ K170)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (≠ Y42), T78 (= T69), S79 (≠ F70), N81 (≠ T72), T82 (≠ S73), Q154 (≠ M145), A192 (≠ M178), G193 (≠ A179), T194 (≠ S180), G195 (= G181), T197 (≠ M183), G242 (≠ D229), S286 (≠ A273), P315 (≠ M298), D316 (≠ T299)
6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
31% identity, 70% coverage: 3:321/456 of query aligns to 9:337/345 of 6c2qA
- binding calcium ion: N180 (vs. gap), D183 (≠ G169), N184 (≠ K170)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (≠ Y42), T78 (= T69), S79 (≠ F70), N81 (≠ T72), T82 (≠ S73), Q154 (≠ M145), A192 (≠ M178), G193 (≠ A179), T194 (≠ S180), G195 (= G181), T197 (≠ M183), G242 (≠ D229), Y245 (≠ A232), S286 (≠ A273), P315 (≠ M298), D316 (≠ T299)
6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
31% identity, 70% coverage: 3:321/456 of query aligns to 9:337/345 of 6c2hA
- binding calcium ion: N180 (vs. gap), D183 (≠ G169), N184 (≠ K170)
- binding pyridoxal-5'-phosphate: K50 (≠ Y42), N81 (≠ T72), A192 (≠ M178), G193 (≠ A179), T194 (≠ S180), G195 (= G181), T197 (≠ M183), G242 (≠ D229), S286 (≠ A273), P315 (≠ M298), D316 (≠ T299)
6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
31% identity, 70% coverage: 3:321/456 of query aligns to 8:336/344 of 6c4pA
- binding calcium ion: N179 (vs. gap), D182 (≠ G169), N183 (≠ K170)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (≠ Y42), N80 (≠ T72), A191 (≠ M178), G192 (≠ A179), T193 (≠ S180), G194 (= G181), T196 (≠ M183), G241 (≠ D229), S285 (≠ A273), P314 (≠ M298), D315 (≠ T299)
P0ABK5 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; S-carboxymethylcysteine synthase; Sulfate starvation-induced protein 5; SSI5; EC 2.5.1.47; EC 4.5.1.5 from Escherichia coli (strain K12) (see 5 papers)
33% identity, 68% coverage: 11:318/456 of query aligns to 14:320/323 of P0ABK5
- K42 (≠ Y42) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_010933579.1 NCBI__GCF_000006985.1:WP_010933579.1
MTNDIFDISDNTPLVLMKQLTRQKRARFMAKLEYMSPCFSHYCRVSGAIVRDAEERGAIH
PGMTLVDWTFGTSGIALAMAAVSRGYKVLLAAPESICREKQEVLRALGAELVLTPSEALP
GDLQSCVDVAENLVRTLPNAWFANMYQNPVSRQVHQDGTGPEIFRQTEGKVTHLFVPMAS
GAMISGIGRYFKSVNPEVQIIGVEPEGSVYGDLHGGKSQGTPSAFQLEDIGAVRPTSFWD
PNVIDRIVQVSDADAFNCGRELLRAEAVFAGGASGAAMAAALREGEAYGDDALVVVMMTD
FGGYDLSRMYNDDWMRRQGFYRKSKTALDQITADDILQRKAHKDLIFAQPEQTLAEVFET
MKQNDVSQMPIVSFGAPIGSISENRILSILIENDSAMNAKVVAFMEKPFPVCQPDATISE
LSEKLQTNASGVLISLSDGRLQLINKSDLIDVLTRK
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