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2VI8

Crystal structure of S172AbsSHMT internal 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 Residues17
DetailsBINDING SITE FOR RESIDUE PLP A1406
ChainResidue
ATYR51
AHIS225
ALYS226
AGLY256
AGLY257
AHOH2099
AHOH2186
AHOH2291
AHOH2304
ASER93
AGLY94
AALA95
AHIS122
AASP197
AALA199
AHIS200
ATHR223

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MPD A1407
ChainResidue
ATYR152
AARG156
AGLU185
AILE186
AGLN321
ALEU322
AHOH2254
AHOH2257
AHOH2458
AHOH2459

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A1408
ChainResidue
APHE131
AGLN135
ATYR136
AILE254

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A1409
ChainResidue
AGLU371
AGLU375
AHOH2414
AHOH2460
AHOH2461

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

219869

PDB entries from 2024-05-15

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