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2VGV

Crystal structure of E53QbsSHMT obtained in the presence of L-allo- Threonine

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 Residues17
DetailsBINDING SITE FOR RESIDUE PLP A1407
ChainResidue
ATYR51
ATHR223
AHIS225
ALYS226
AGLY256
AGLY257
AGLY1408
AHOH2218
AHOH2219
ASER93
AGLY94
AALA95
AHIS122
ASER172
AASP197
AALA199
AHIS200

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GLY A1408
ChainResidue
ASER31
AGLN53
ATYR61
AHIS122
AHIS200
ALYS226
AARG357
APLP1407

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A1409
ChainResidue
ATYR152
AARG156
ALEU322
AHOH2176

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

218853

PDB entries from 2024-04-24

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