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4WXG

Crystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L-Threonine and Glycine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006544biological_processglycine metabolic process
A0006545biological_processglycine biosynthetic process
A0006563biological_processL-serine metabolic 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
C0004372molecular_functionglycine hydroxymethyltransferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006544biological_processglycine metabolic process
C0006545biological_processglycine biosynthetic process
C0006563biological_processL-serine metabolic process
C0006730biological_processone-carbon metabolic process
C0008652biological_processamino acid biosynthetic process
C0016740molecular_functiontransferase activity
C0019264biological_processglycine biosynthetic process from serine
C0030170molecular_functionpyridoxal phosphate binding
C0035999biological_processtetrahydrofolate interconversion
C0046653biological_processtetrahydrofolate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue 2BO A 501
ChainResidue
ASER35
ATHR227
AHIS229
ALYS230
AARG363
AHOH636
AHOH681
CTYR55
CGLU57
CTYR65
CGLY261
ASER97
CGLY262
CHOH602
AGLY98
ASER99
AHIS126
ASER176
AASP201
AALA203
AHIS204

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 502
ChainResidue
APHE301
AASN302
AHIS304
APHE307

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 503
ChainResidue
ALEU154
ATYR156
AARG180
AASP183
AHOH664
AHOH664
AHOH683
AHOH711
AHOH752

site_idAC4
Number of Residues21
Detailsbinding site for residue 2BO C 501
ChainResidue
ATYR55
AGLU57
ATYR65
AGLY261
AGLY262
AHOH601
CSER35
CSER97
CGLY98
CSER99
CHIS126
CSER176
CASP201
CALA203
CHIS204
CTHR227
CHIS229
CLYS230
CARG363
CHOH675
CHOH713

site_idAC5
Number of Residues4
Detailsbinding site for residue NA C 502
ChainResidue
CPHE301
CASN302
CHIS304
CPHE307

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVtTTTTHKTLrGPRGG
ChainResidueDetails
AHIS222-GLY238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Plays an important role in substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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