2VGS

Crystal structure of E53QbsSHMT internal aldimine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004372	molecular_function	glycine hydroxymethyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006545	biological_process	glycine biosynthetic process
A	0006565	biological_process	L-serine catabolic process
A	0006730	biological_process	one-carbon metabolic process
A	0008270	molecular_function	zinc ion binding
A	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0019264	biological_process	glycine biosynthetic process from serine
A	0030170	molecular_function	pyridoxal phosphate binding
A	0035999	biological_process	tetrahydrofolate interconversion
A	0046653	biological_process	tetrahydrofolate metabolic process
A	0046655	biological_process	folic acid metabolic process
A	0050897	molecular_function	cobalt ion binding
A	0070905	molecular_function	serine binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A1407

Chain	Residue
A	TYR51
A	THR223
A	HIS225
A	LYS226
A	GLY256
A	GLY257
A	HOH2248
A	SER93
A	GLY94
A	ALA95
A	HIS122
A	ALA171
A	ASP197
A	ALA199
A	HIS200

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD A1408

Chain	Residue
A	TYR152
A	ARG156
A	GLU185
A	LEU322
A	HOH2139
A	HOH2249

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Functional Information from PROSITE/UniProt

site_id	PS00096
Number of Residues	17
Details	SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HFvTTTTHKTLrGPRGG

Chain	Residue	Details
A	HIS218-GLY234

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