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6UXH

Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Essex complexed with PLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO B 501
ChainResidue
AGLY52
AHOH613
BGLY52
BHOH604
BHOH638
BHOH661

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRAG
ChainResidueDetails
AASP236-GLY252

226707

PDB entries from 2024-10-30

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