8SUI

Joint X-ray/neutron structure of Thermus thermophilus serine hydroxymethyltransferase (TthSHMT) in internal aldimine state with L-Ser bound in a pre-Michalis complex

Functional Information from GO Data

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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS218-GLY234

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|Ref.2

Chain	Residue	Details
A	TYR51
A	GLY94
A	SER172
A	HIS200
A	HIS225
A	GLY258
B	TYR1051
B	GLY1094
B	SER1172
B	HIS1200
B	HIS1225
B	GLY1258

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	LEU117
A	GLY121
A	GLU242
B	LEU1117
B	GLY1121
B	GLU1242

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	HIS225
B	HIS1225

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.2

Chain	Residue	Details
A	LLP226
B	LLP1226

---