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2W7G

Crystal structure of Y51FbsSHMT L-allo-Threonine extrnal aldimine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006565biological_processL-serine catabolic process
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
A0046655biological_processfolic acid metabolic process
A0050897molecular_functioncobalt ion binding
A0070905molecular_functionserine binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
APHE51
AALA199
AHIS200
ATHR223
AHIS225
ALYS226
AGLY257
AALO601
AHOH2068
AHOH2215
AHOH2217
AGLU53
AHOH2330
AHOH2331
AHOH2332
AHOH2333
ASER93
AGLY94
AALA95
AHIS122
AALA171
ASER172
AASP197

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ALO A 601
ChainResidue
ASER31
APHE51
AGLU53
ATYR61
AHIS122
AHIS200
ALYS226
AARG357
APLP501

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 701
ChainResidue
ATYR152
AARG156
AGLU185
ALEU322
AHOH2335
AHOH2336
AHOH2337

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 801
ChainResidue
AGLU372
AHOH2338
AHOH2339

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HFvTTTTHKTLrGPRGG
ChainResidueDetails
AHIS218-GLY234

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PDB entries from 2024-07-24

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