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2VGW

Crystal structure of E53QbsSHMT obtained in the presence of glycine and 5-fomyl tetrahydrofolate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006730biological_processone-carbon metabolic process
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
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE PLP A1407
ChainResidue
ATYR51
AALA199
AHIS200
ATHR223
AHIS225
ALYS226
AGLY256
AGLY257
AGLY1408
AHOH2281
AHOH2282
AGLN53
AHOH2283
AHOH2284
ASER93
AGLY94
AALA95
AHIS122
AALA171
ASER172
AASP197

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GLY A1408
ChainResidue
ASER31
ATYR51
ATYR61
ASER172
AHIS200
ALYS226
AARG357
APLP1407

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A1409
ChainResidue
ATYR152
AARG156
AGLU185
ALEU322
AHOH2285
AHOH2286
AHOH2287

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PO4 A1410
ChainResidue
AHOH2288

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 2024-11-06

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