Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3GBX

Serine hydroxymethyltransferase from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
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
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006545biological_processglycine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
B0046653biological_processtetrahydrofolate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 501
ChainResidue
BTYR196
BGLU247
BLYS251

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTTTTHKTLaGPRGG
ChainResidueDetails
AHIS221-GLY237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALEU121
AGLY125
ASER355
BLEU121
BGLY125
BSER355

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AHIS228
BHIS228

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALYS229
BLYS229

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
ATHR226
ALYS229

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BTHR226
BLYS229

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
ALYS229
AHIS203

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BLYS229
BHIS203

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon