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7V3D

Complex structure of serine hydroxymethyltransferase from Enterococcus faecium and its inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0006545biological_processglycine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0008652biological_processamino acid biosynthetic process
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
B0003824molecular_functioncatalytic activity
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0006545biological_processglycine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0008652biological_processamino acid biosynthetic process
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0032259biological_processmethylation
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DItTTTTHKTLrGPRGG
ChainResidueDetails
AASP218-GLY234

222415

PDB entries from 2024-07-10

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