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Crystal structure of a glycine hydroxymethyltransferase from Acinetobacter baumannii

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0019264biological_processobsolete glycine biosynthetic process from L-serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DVtTTTTHKTLrGPRSG
ChainResidueDetails
AASP221-GLY237

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PDB entries from 2026-04-08

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