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5Z0Y

Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase (SHMT) from Pichia pastoris

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0006565biological_processL-serine catabolic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0008270molecular_functionzinc ion binding
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
A0046655biological_processfolic acid metabolic process
A0050897molecular_functioncobalt ion binding
A0070905molecular_functionserine binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 501
ChainResidue
ALEU98
AASP99
AARG102
ATRP103
AHOH602
AHOH605

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRGA
ChainResidueDetails
AASP241-ALA257

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PDB entries from 2024-10-16

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