SitesBLAST
Comparing Dsui_2254 FitnessBrowser__PS:Dsui_2254 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)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
64% identity, 93% coverage: 30:432/433 of query aligns to 15:407/407 of Q5SI56
- Y51 (= Y66) binding
- GS 94:95 (= GS 109:110) binding
- S172 (= S187) binding
- H200 (= H215) binding
- H225 (= H240) binding
- K226 (= K241) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G273) binding
8suiB Joint x-ray/neutron structure of thermus thermophilus serine hydroxymethyltransferase (tthshmt) in internal aldimine state with l- ser bound in a pre-michalis complex (see paper)
64% identity, 93% coverage: 30:432/433 of query aligns to 10:402/402 of 8suiB
8ssyA Room-temperature x-ray structure of thermus thermophilus serine hydroxymethyltransferase (shmt) bound with d-ser in a pseudo- michaelis complex (see paper)
64% identity, 93% coverage: 30:432/433 of query aligns to 10:402/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
64% identity, 93% coverage: 30:432/433 of query aligns to 10:402/402 of 2dkjA
- active site: Y46 (= Y66), E48 (= E68), D192 (= D212), T218 (= T238), K221 (= K241), R227 (= R247)
- binding pyridoxal-5'-phosphate: S88 (= S108), G89 (= G109), S90 (= S110), H117 (= H137), S167 (= S187), D192 (= D212), A194 (= A214), H220 (= H240), K221 (= K241)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
58% identity, 95% coverage: 19:431/433 of query aligns to 7:413/418 of 6ymfA
- active site: Y54 (= Y66), E56 (= E68), D200 (= D212), T226 (= T238), K229 (= K241), R235 (= R247)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S46), S96 (= S108), G97 (= G109), A98 (≠ S110), H125 (= H137), S175 (= S187), D200 (= D212), A202 (= A214), H203 (= H215), T226 (= T238), K229 (= K241), R361 (= R373)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
59% identity, 97% coverage: 12:431/433 of query aligns to 1:412/414 of 4ot8A
- active site: Y55 (= Y66), E57 (= E68), D200 (= D212), T226 (= T238), K229 (= K241), R235 (= R247)
- binding pyridoxal-5'-phosphate: S97 (= S108), G98 (= G109), S99 (= S110), H126 (= H137), D200 (= D212), A202 (= A214), H203 (= H215), K229 (= K241)
- binding serine: S35 (= S46), E57 (= E68), Y65 (= Y76), H126 (= H137), H203 (= H215), R360 (= R373)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
58% identity, 95% coverage: 19:431/433 of query aligns to 7:413/420 of 6ymdA
- active site: Y54 (= Y66), E56 (= E68), D200 (= D212), T226 (= T238), K229 (= K241), R235 (= R247)
- binding malonate ion: S34 (= S46), Y54 (= Y66), E56 (= E68), Y64 (= Y76), H125 (= H137), H203 (= H215), K229 (= K241), R361 (= R373)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y66), S96 (= S108), G97 (= G109), A98 (≠ S110), H125 (= H137), Y174 (≠ G186), S175 (= S187), D200 (= D212), A202 (= A214), T226 (= T238), K229 (= K241), G261 (= G273)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
59% identity, 97% coverage: 12:431/433 of query aligns to 3:414/416 of 4n0wA
- active site: Y57 (= Y66), E59 (= E68), D202 (= D212), T228 (= T238), K231 (= K241), R237 (= R247)
- binding pyridoxal-5'-phosphate: S99 (= S108), G100 (= G109), S101 (= S110), H128 (= H137), D202 (= D212), A204 (= A214), H205 (= H215), K231 (= K241)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
63% identity, 86% coverage: 23:396/433 of query aligns to 8:380/405 of 1kl2A
- active site: Y51 (= Y66), E53 (= E68), D197 (= D212), T223 (= T238), K226 (= K241), R232 (= R247)
- binding N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid: E53 (= E68), Y60 (= Y75), G121 (= G136), H122 (= H137), S172 (= S187), F251 (= F267), N341 (= N357)
- binding glycine: S31 (= S46), Y51 (= Y66), Y61 (= Y76), H200 (= H215), R357 (= R373)
- binding pyridoxal-5'-phosphate: S93 (= S108), G94 (= G109), A95 (≠ S110), H122 (= H137), S172 (= S187), D197 (= D212), A199 (= A214), H200 (= H215), T223 (= T238), H225 (= H240), K226 (= K241)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
63% identity, 86% coverage: 23:396/433 of query aligns to 8:380/405 of 1kl1A
- active site: Y51 (= Y66), E53 (= E68), D197 (= D212), T223 (= T238), K226 (= K241), R232 (= R247)
- binding glycine: S31 (= S46), H122 (= H137), R357 (= R373)
- binding pyridoxal-5'-phosphate: S93 (= S108), G94 (= G109), A95 (≠ S110), H122 (= H137), A171 (≠ G186), S172 (= S187), D197 (= D212), A199 (= A214), H200 (= H215), T223 (= T238), H225 (= H240), K226 (= K241)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
63% identity, 86% coverage: 23:396/433 of query aligns to 8:380/405 of 1kkpA
- active site: Y51 (= Y66), E53 (= E68), D197 (= D212), T223 (= T238), K226 (= K241), R232 (= R247)
- binding pyridoxal-5'-phosphate: S93 (= S108), G94 (= G109), A95 (≠ S110), H122 (= H137), S172 (= S187), D197 (= D212), A199 (= A214), H200 (= H215), K226 (= K241)
- binding serine: S31 (= S46), H122 (= H137), R357 (= R373)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
63% identity, 86% coverage: 23:396/433 of query aligns to 8:380/405 of 1kkjA
- active site: Y51 (= Y66), E53 (= E68), D197 (= D212), T223 (= T238), K226 (= K241), R232 (= R247)
- binding pyridoxal-5'-phosphate: S93 (= S108), G94 (= G109), A95 (≠ S110), H122 (= H137), S172 (= S187), D197 (= D212), A199 (= A214), H200 (= H215), T223 (= T238), H225 (= H240), K226 (= K241)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
60% identity, 95% coverage: 19:431/433 of query aligns to 3:407/409 of 4otlA
- active site: Y50 (= Y66), E52 (= E68), D195 (= D212), T221 (= T238), K224 (= K241), R230 (= R247)
- binding glycine: S30 (= S46), Y50 (= Y66), Y60 (= Y76), H121 (= H137), K224 (= K241), R355 (= R373)
- binding pyridoxal-5'-phosphate: S92 (= S108), G93 (= G109), S94 (= S110), H121 (= H137), S170 (= S187), D195 (= D212), A197 (= A214), H198 (= H215), K224 (= K241)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
63% identity, 86% coverage: 23:396/433 of query aligns to 8:380/405 of 2vmyA
- active site: Y51 (= Y66), E53 (= E68), D197 (= D212), T223 (= T238), K226 (= K241), R232 (= R247)
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: E53 (= E68), Y60 (= Y75), Y61 (= Y76), L117 (= L132), G121 (= G136), H122 (= H137), L123 (= L138), S172 (= S187), K248 (≠ S264), F251 (= F267), N341 (= N357), S349 (≠ K365), P350 (= P366), G351 (≠ M367), R357 (= R373)
- binding glycine: S31 (= S46), Y51 (= Y66), Y61 (= Y76), H200 (= H215), K226 (= K241), R357 (= R373)
- binding pyridoxal-5'-phosphate: Y51 (= Y66), S93 (= S108), G94 (= G109), A95 (≠ S110), H122 (= H137), S172 (= S187), D197 (= D212), A199 (= A214), H200 (= H215), T223 (= T238), K226 (= K241), G257 (= G273)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
63% identity, 86% coverage: 23:396/433 of query aligns to 8:380/405 of 2vmxA
- active site: Y51 (= Y66), E53 (= E68), D197 (= D212), T223 (= T238), K226 (= K241), R232 (= R247)
- binding allo-threonine: S31 (= S46), H122 (= H137), H200 (= H215), R357 (= R373)
- binding pyridoxal-5'-phosphate: S93 (= S108), G94 (= G109), A95 (≠ S110), H122 (= H137), S172 (= S187), D197 (= D212), A199 (= A214), H200 (= H215), T223 (= T238), K226 (= K241)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
58% identity, 95% coverage: 22:431/433 of query aligns to 5:409/409 of 7x5nA
- binding (4R)-6-azanyl-4-[3-(hydroxymethyl)-5-phenyl-phenyl]-3-methyl-4-propan-2-yl-1H-pyrano[2,3-c]pyrazole-5-carbonitrile: E51 (= E68), Y58 (= Y75), Y59 (= Y76), L115 (= L132), G119 (= G136), H120 (= H137), L121 (= L138), K340 (= K356), N341 (= N357), S342 (≠ A358), P350 (= P366), F351 (≠ M367), R357 (= R373)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S46), Y49 (= Y66), E51 (= E68), Y59 (= Y76), S91 (= S108), G92 (= G109), S93 (= S110), H120 (= H137), S170 (= S187), D195 (= D212), A197 (= A214), H198 (= H215), K224 (= K241), R357 (= R373)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
58% identity, 95% coverage: 22:431/433 of query aligns to 5:409/409 of 7v3dA
- binding (4R)-6-azanyl-4-[3-(hydroxymethyl)-5-phenyl-phenyl]-3-methyl-4-propan-2-yl-1H-pyrano[2,3-c]pyrazole-5-carbonitrile: E51 (= E68), Y58 (= Y75), L115 (= L132), G119 (= G136), H120 (= H137), L121 (= L138), K340 (= K356), S342 (≠ A358), P350 (= P366), F351 (≠ M367), R357 (= R373)
- binding pyridoxal-5'-phosphate: Y49 (= Y66), S91 (= S108), G92 (= G109), S93 (= S110), H120 (= H137), S170 (= S187), D195 (= D212), A197 (= A214), K224 (= K241), G255 (= G272)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
58% identity, 95% coverage: 22:431/433 of query aligns to 6:410/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S46), Y50 (= Y66), Y60 (= Y76), S92 (= S108), G93 (= G109), S94 (= S110), H121 (= H137), S171 (= S187), D196 (= D212), A198 (= A214), H199 (= H215), K225 (= K241), R358 (= R373)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E68), Y59 (= Y75), L116 (= L132), G119 (= G135), G120 (= G136), H121 (= H137), S171 (= S187), P252 (= P268), N342 (= N357), P351 (= P366)
4wxgA Crystal structure of l-serine hydroxymethyltransferase in complex with a mixture of l-threonine and glycine (see paper)
58% identity, 95% coverage: 22:431/433 of query aligns to 5:409/410 of 4wxgA
- active site: T43 (≠ S60), L45 (= L62), G189 (= G206), A215 (= A232), T218 (≠ V235), R230 (= R247)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine: S29 (= S46), Y49 (= Y66), E51 (= E68), Y59 (= Y76), S91 (= S108), G92 (= G109), S93 (= S110), H120 (= H137), S170 (= S187), D195 (= D212), A197 (= A214), H198 (= H215), T221 (= T238), K224 (= K241), G255 (= G272), R357 (= R373)
4wxfA Crystal structure of l-serine hydroxymethyltransferase in complex with glycine (see paper)
58% identity, 95% coverage: 22:431/433 of query aligns to 5:409/410 of 4wxfA
- active site: T43 (≠ S60), L45 (= L62), G189 (= G206), A215 (= A232), T218 (≠ V235), R230 (= R247)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S29 (= S46), Y49 (= Y66), Y59 (= Y76), S91 (= S108), G92 (= G109), S93 (= S110), H120 (= H137), S170 (= S187), D195 (= D212), A197 (= A214), H198 (= H215), H223 (= H240), K224 (= K241), G255 (= G272), R357 (= R373)
Query Sequence
>Dsui_2254 FitnessBrowser__PS:Dsui_2254
MNNPNDLPRPPYDQAPGALGRIDPEAARYVAAEYARQRHSIELIASENIVSRAVLEMQGS
VLTNKYAEGYPGRRYYGGCGPVDGVEALAIARAKGLFGCAYANVQPHSGSQANQAVYLAL
LQPGDTILGLGLAAGGHLTHGAPMNQSGKWFRGVAYGVRADDHRIDMAQVEQLAYEYRPK
LIIAGGSAYSRILDFAEFRRIADRVGARLLVDMAHFAGLVAGGAHPSPLPYADVVTSTTH
KTLRGPRGGLILSNDAALGKAIDSAVFPGLQGGPLMHVIGAKAVAFGEALQPEFRSYAAR
VVENAQALADALAAGGLRIVSGGTDTHLAVADLRPLNLTGNVAEKALERVGITLNKNAIP
HDPQKPMVTSGIRVGSPAGTSRGFRTAEFRLIGGLIVHLLEALAANPEAPDPAVAAAVRA
QVAELCRRFPLPY
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