6TI1

SHMT from Streptococcus thermophilus Tyr55Ser variant in complex with PLP/L-Threonine/Lys230 gem diamine complex

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL A 501

Chain	Residue
A	TYR156
A	ARG180
A	ASP183
A	HOH645
A	HOH645
A	HOH653
A	HOH664

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site_id	AC2
Number of Residues	23
Details	binding site for residue 2BO A 502

Chain	Residue
A	GLY98
A	SER99
A	HIS126
A	SER176
A	ASP201
A	ALA203
A	HIS204
A	HIS229
A	LYS230
A	ARG363
A	HOH666
A	HOH682
A	HOH721
A	HOH760
C	SER55
C	GLU57
C	TYR65
C	GLY261
C	GLY262
C	HOH676
C	HOH708
A	SER35
A	SER97

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 503

Chain	Residue
A	ALA203
A	ALA206
A	HIS229
A	LYS230
A	THR231
A	LEU232

---

site_id	AC4
Number of Residues	23
Details	binding site for Di-peptide 2BO C 501 and LYS C 230

Chain	Residue
A	GLU57
A	TYR65
A	GLY261
A	GLY262
C	SER35
C	ASN37
C	SER97
C	GLY98
C	SER99
C	HIS126
C	SER176
C	ASP201
C	ALA203
C	HIS204
C	HIS229
C	THR231
C	LEU232
C	ARG233
C	ARG363
C	HOH650
C	HOH652
C	HOH674
C	HOH714

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS222-GLY238

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	SER355
C	LEU121
C	GLY125
C	SER355
A	LEU121
A	GLY125

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	HIS229
C	HIS229

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	LYS230
C	LYS230

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