SitesBLAST
Comparing 3607407 FitnessBrowser__Dino:3607407 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)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
64% identity, 96% coverage: 14:428/431 of query aligns to 2:408/409 of 4otlA
- active site: Y50 (= Y62), E52 (= E64), D195 (= D208), T221 (= T234), K224 (= K237), R230 (= R243)
- binding glycine: S30 (= S42), Y50 (= Y62), Y60 (= Y72), H121 (= H133), K224 (= K237), R355 (= R369)
- binding pyridoxal-5'-phosphate: S92 (= S104), G93 (= G105), S94 (= S106), H121 (= H133), S170 (= S183), D195 (= D208), A197 (= A210), H198 (= H211), K224 (= K237)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
64% identity, 96% coverage: 14:428/431 of query aligns to 9:415/416 of 4n0wA
- active site: Y57 (= Y62), E59 (= E64), D202 (= D208), T228 (= T234), K231 (= K237), R237 (= R243)
- binding pyridoxal-5'-phosphate: S99 (= S104), G100 (= G105), S101 (= S106), H128 (= H133), D202 (= D208), A204 (= A210), H205 (= H211), K231 (= K237)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
64% identity, 96% coverage: 14:428/431 of query aligns to 7:413/414 of 4ot8A
- active site: Y55 (= Y62), E57 (= E64), D200 (= D208), T226 (= T234), K229 (= K237), R235 (= R243)
- binding pyridoxal-5'-phosphate: S97 (= S104), G98 (= G105), S99 (= S106), H126 (= H133), D200 (= D208), A202 (= A210), H203 (= H211), K229 (= K237)
- binding serine: S35 (= S42), E57 (= E64), Y65 (= Y72), H126 (= H133), H203 (= H211), R360 (= R369)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
59% identity, 97% coverage: 15:431/431 of query aligns to 7:417/418 of 6ymfA
- active site: Y54 (= Y62), E56 (= E64), D200 (= D208), T226 (= T234), K229 (= K237), R235 (= R243)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S42), S96 (= S104), G97 (= G105), A98 (≠ S106), H125 (= H133), S175 (= S183), D200 (= D208), A202 (= A210), H203 (= H211), T226 (= T234), K229 (= K237), R361 (= R369)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
59% identity, 97% coverage: 15:431/431 of query aligns to 7:417/420 of 6ymdA
- active site: Y54 (= Y62), E56 (= E64), D200 (= D208), T226 (= T234), K229 (= K237), R235 (= R243)
- binding malonate ion: S34 (= S42), Y54 (= Y62), E56 (= E64), Y64 (= Y72), H125 (= H133), H203 (= H211), K229 (= K237), R361 (= R369)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y62), S96 (= S104), G97 (= G105), A98 (≠ S106), H125 (= H133), Y174 (≠ G182), S175 (= S183), D200 (= D208), A202 (= A210), T226 (= T234), K229 (= K237), G261 (= G269)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
62% identity, 89% coverage: 14:396/431 of query aligns to 3:385/407 of Q5SI56
- Y51 (= Y62) binding
- GS 94:95 (= GS 105:106) binding
- S172 (= S183) binding
- H200 (= H211) binding
- H225 (= H236) binding
- K226 (= K237) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G269) 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)
62% identity, 88% coverage: 18:396/431 of query aligns to 2:380/402 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)
62% identity, 88% coverage: 18:396/431 of query aligns to 2:380/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
62% identity, 88% coverage: 18:396/431 of query aligns to 2:380/402 of 2dkjA
- active site: Y46 (= Y62), E48 (= E64), D192 (= D208), T218 (= T234), K221 (= K237), R227 (= R243)
- binding pyridoxal-5'-phosphate: S88 (= S104), G89 (= G105), S90 (= S106), H117 (= H133), S167 (= S183), D192 (= D208), A194 (= A210), H220 (= H236), K221 (= K237)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
62% identity, 88% coverage: 15:392/431 of query aligns to 4:380/405 of 1kl2A
- active site: Y51 (= Y62), E53 (= E64), D197 (= D208), T223 (= T234), K226 (= K237), R232 (= R243)
- 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 (= E64), Y60 (= Y71), G121 (= G132), H122 (= H133), S172 (= S183), F251 (= F263), N341 (= N353)
- binding glycine: S31 (= S42), Y51 (= Y62), Y61 (= Y72), H200 (= H211), R357 (= R369)
- binding pyridoxal-5'-phosphate: S93 (= S104), G94 (= G105), A95 (≠ S106), H122 (= H133), S172 (= S183), D197 (= D208), A199 (= A210), H200 (= H211), T223 (= T234), H225 (= H236), K226 (= K237)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
62% identity, 88% coverage: 15:392/431 of query aligns to 4:380/405 of 1kl1A
- active site: Y51 (= Y62), E53 (= E64), D197 (= D208), T223 (= T234), K226 (= K237), R232 (= R243)
- binding glycine: S31 (= S42), H122 (= H133), R357 (= R369)
- binding pyridoxal-5'-phosphate: S93 (= S104), G94 (= G105), A95 (≠ S106), H122 (= H133), A171 (≠ G182), S172 (= S183), D197 (= D208), A199 (= A210), H200 (= H211), T223 (= T234), H225 (= H236), K226 (= K237)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
62% identity, 88% coverage: 15:392/431 of query aligns to 4:380/405 of 1kkpA
- active site: Y51 (= Y62), E53 (= E64), D197 (= D208), T223 (= T234), K226 (= K237), R232 (= R243)
- binding pyridoxal-5'-phosphate: S93 (= S104), G94 (= G105), A95 (≠ S106), H122 (= H133), S172 (= S183), D197 (= D208), A199 (= A210), H200 (= H211), K226 (= K237)
- binding serine: S31 (= S42), H122 (= H133), R357 (= R369)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
62% identity, 88% coverage: 15:392/431 of query aligns to 4:380/405 of 1kkjA
- active site: Y51 (= Y62), E53 (= E64), D197 (= D208), T223 (= T234), K226 (= K237), R232 (= R243)
- binding pyridoxal-5'-phosphate: S93 (= S104), G94 (= G105), A95 (≠ S106), H122 (= H133), S172 (= S183), D197 (= D208), A199 (= A210), H200 (= H211), T223 (= T234), H225 (= H236), K226 (= K237)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
59% identity, 96% coverage: 17:428/431 of query aligns to 5:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S42), Y50 (= Y62), Y60 (= Y72), S92 (= S104), G93 (= G105), S94 (= S106), H121 (= H133), S171 (= S183), D196 (= D208), A198 (= A210), H199 (= H211), K225 (= K237), R358 (= R369)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E64), Y59 (= Y71), L116 (= L128), G119 (= G131), G120 (= G132), H121 (= H133), S171 (= S183), P252 (= P264), N342 (= N353), P351 (= P362)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
59% identity, 95% coverage: 17:427/431 of query aligns to 4:409/409 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 (= E64), Y58 (= Y71), Y59 (= Y72), L115 (= L128), G119 (= G132), H120 (= H133), L121 (= L134), K340 (= K352), N341 (= N353), S342 (≠ G354), P350 (= P362), F351 (≠ M363), R357 (= R369)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S42), Y49 (= Y62), E51 (= E64), Y59 (= Y72), S91 (= S104), G92 (= G105), S93 (= S106), H120 (= H133), S170 (= S183), D195 (= D208), A197 (= A210), H198 (= H211), K224 (= K237), R357 (= R369)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
59% identity, 95% coverage: 17:427/431 of query aligns to 4:409/409 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 (= E64), Y58 (= Y71), L115 (= L128), G119 (= G132), H120 (= H133), L121 (= L134), K340 (= K352), S342 (≠ G354), P350 (= P362), F351 (≠ M363), R357 (= R369)
- binding pyridoxal-5'-phosphate: Y49 (= Y62), S91 (= S104), G92 (= G105), S93 (= S106), H120 (= H133), S170 (= S183), D195 (= D208), A197 (= A210), K224 (= K237), G255 (= G268)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
62% identity, 88% coverage: 15:392/431 of query aligns to 4:380/405 of 2vmyA
- active site: Y51 (= Y62), E53 (= E64), D197 (= D208), T223 (= T234), K226 (= K237), R232 (= R243)
- 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 (= E64), Y60 (= Y71), Y61 (= Y72), L117 (= L128), G121 (= G132), H122 (= H133), L123 (= L134), S172 (= S183), K248 (≠ S260), F251 (= F263), N341 (= N353), S349 (≠ K361), P350 (= P362), G351 (≠ M363), R357 (= R369)
- binding glycine: S31 (= S42), Y51 (= Y62), Y61 (= Y72), H200 (= H211), K226 (= K237), R357 (= R369)
- binding pyridoxal-5'-phosphate: Y51 (= Y62), S93 (= S104), G94 (= G105), A95 (≠ S106), H122 (= H133), S172 (= S183), D197 (= D208), A199 (= A210), H200 (= H211), T223 (= T234), K226 (= K237), G257 (= G269)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
62% identity, 88% coverage: 15:392/431 of query aligns to 4:380/405 of 2vmxA
- active site: Y51 (= Y62), E53 (= E64), D197 (= D208), T223 (= T234), K226 (= K237), R232 (= R243)
- binding allo-threonine: S31 (= S42), H122 (= H133), H200 (= H211), R357 (= R369)
- binding pyridoxal-5'-phosphate: S93 (= S104), G94 (= G105), A95 (≠ S106), H122 (= H133), S172 (= S183), D197 (= D208), A199 (= A210), H200 (= H211), T223 (= T234), K226 (= K237)
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
58% identity, 96% coverage: 14:428/431 of query aligns to 7:416/417 of 1dfoB
- active site: Y55 (= Y62), E57 (= E64), D200 (= D208), T226 (= T234), K229 (= K237), R235 (= R243)
- 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: E57 (= E64), Y64 (= Y71), Y65 (= Y72), L121 (= L128), G125 (= G132), H126 (= H133), L127 (= L134), S175 (= S183), S245 (≠ D251), E247 (≠ A253), N347 (= N353), S355 (≠ K361), P356 (= P362), F357 (≠ M363)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S42), Y55 (= Y62), Y65 (= Y72), S97 (= S104), G98 (= G105), S99 (= S106), H126 (= H133), F174 (≠ G182), S175 (= S183), D200 (= D208), A202 (= A210), H203 (= H211), K229 (= K237), G262 (= G268), R363 (= R369)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
58% identity, 96% coverage: 14:428/431 of query aligns to 7:416/417 of P0A825
- K54 (= K61) modified: N6-acetyllysine
- Y55 (= Y62) mutation to F: 50 and 15-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 4-fold decrease in the catalytic efficiency.
- K62 (≠ R69) modified: N6-succinyllysine
- Y65 (= Y72) mutation to F: Decrease in catalytic activity.
- L85 (= L92) mutation to A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-276.
- P214 (= P222) mutation to A: No significant difference in catalytic efficiency and affinity compared to the wild-type.; mutation to G: No significant difference in catalytic efficiency and affinity compared to the wild-type.
- P216 (= P224) mutation to A: No significant difference in catalytic efficiency and affinity compared to the wild-type. Alteration in the folding rate.; mutation to G: Important decrease in affinity and catalytic efficiency. Severely compromised in folding into a catalytically competent enzyme.
- P218 (= P226) mutation to A: No significant difference in catalytic efficiency and affinity compared to the wild-type.; mutation to G: No significant difference in catalytic efficiency and affinity compared to the wild-type.
- H228 (= H236) Plays an important role in substrate specificity; binding ; mutation H->D,N: Utilize substrates and substrate analogs more effectively for a variety of alternate non-physiological reactions.
- K229 (= K237) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R243) binding ; mutation to K: 1500- and 20-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 15-fold decrease in the catalytic efficiency.; mutation to L: 450- and 11-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 60-fold decrease in the catalytic efficiency.; mutation to Q: 900- and 17-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 30-fold decrease in the catalytic efficiency.
- K242 (≠ D250) modified: N6-succinyllysine
- K250 (= K256) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P264) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P270) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F282) mutation to A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-85.
- K277 (≠ G283) modified: N6-succinyllysine
- K285 (= K291) modified: N6-acetyllysine
- K293 (≠ E299) modified: N6-succinyllysine
- K331 (≠ N337) modified: N6-succinyllysine
- K346 (= K352) modified: N6-succinyllysine
- K354 (≠ E360) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R369) mutation to A: It does not bind serine and glycine and shows no activity with serine as the substrate.; mutation to K: Exhibits only 0.03% of the catalytic activity of the wild-type and a 15-fold reduction in affinity for glycine and serine.
- R372 (= R378) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (≠ G381) modified: N6-acetyllysine
Query Sequence
>3607407 FitnessBrowser__Dino:3607407
MNAPHRDNGFFTESLATRDAELFGAITKELGRQRDEIELIASENIVSAAVMEAQGSVLTN
KYAEGYPGRRYYGGCQYVDIAEELAIDRARQLFGCAFANVQPNSGSQANQGVFTALLQPG
DTILGMSLDAGGHLTHGAKPNQSGKWFNAVQYGVRQDTLDVDYDQIAALAAEHKPKMIIA
GGSAIPRIIDFARIREIADSVGAWVLVDMAHFAGLVAAGHYPSPFPHAHVATTTTHKTLR
GPRGGMILTDDEALAKKFNSAIFPGIQGGPLMHVIAGKAVAFGEALRPEFKTYQAQVIEN
AQALADQLMQGGLDIVTGGTDTHVLLVDLRPKGVKGNATEKALGRAHITCNKNGIPFDTE
KPMITSGIRLGSPAGTTRGFGTPEFRQIADWIVRVVDGLAANGEDGNAEVEAAVRAEVLE
LCGRFPIYPNL
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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