Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PGY

Serine hydroxymethyltransferase from Staphylococcus aureus, S95P mutant.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CIT B 501

Chain	Residue
A	TYR51
B	HOH424
B	HOH791
A	GLY256
A	GLY257
B	GLY94
B	PRO95
B	THR223
B	HIS225
B	LYS226
B	ARG232

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CIT B 502

Chain	Residue
B	ILE75
B	LYS79
B	GLU85
B	HIS86
B	VAL87
B	GLU240
B	LYS243

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIT D 503

Chain	Residue
C	GLY94
C	PRO95
C	THR223
C	HIS225
C	LYS226
C	ARG232
C	HOH493
D	TYR51
D	GLU53
D	GLY256
D	GLY257
D	HOH447
D	HOH526

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT D 504

Chain	Residue
D	ILE75
D	LYS79
D	GLU85
D	HIS86
D	VAL87
D	GLU240
D	LYS243
D	HOH898
D	HOH1055

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CIT A 505

Chain	Residue
A	ILE75
A	LYS79
A	GLU85
A	HIS86
A	VAL87
A	GLU240
A	LYS243

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CIT B 506

Chain	Residue
A	GLY94
A	PRO95
A	THR223
A	HIS225
A	LYS226
A	ARG232
B	TYR51
B	GLU53
B	GLY256
B	GLY257
B	HOH417
B	HOH438
B	HOH468
B	HOH522

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CIT D 507

Chain	Residue
C	GLU53
C	GLY256
C	GLY257
D	GLY94
D	PRO95
D	THR223
D	HIS225
D	LYS226
D	ARG232
D	HOH438
D	HOH643
D	HOH800

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT C 508

Chain	Residue
C	ILE75
C	LYS79
C	GLU85
C	HIS86
C	VAL87
C	GLU240
C	LYS243
C	HOH801

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GLY B 509

Chain	Residue
B	THR366
B	LEU410
B	TYR411
B	HOH992

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GLY A 510

Chain	Residue
A	GLU27
A	ASN33
A	PHE34
A	ALA363
A	HOH469
A	HOH804
B	ASN49

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GLY B 511

Chain	Residue
B	SER334
B	GLU391
B	LEU394
B	GLN395
B	LYS398

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 512

Chain	Residue
C	GLU32
C	HIS200
C	LYS226
D	TYR51
C	ALA30
C	SER31

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 513

Chain	Residue
A	ASP153
C	GLU299
C	SER382
C	LEU383
C	LYS386
C	HOH446
C	HOH492

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP218-GLY234

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	LEU117
A	GLY121
B	LEU117
B	GLY121
C	LEU117
C	GLY121
D	LEU117
D	GLY121

site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Plays an important role in substrate specificity => ECO:0000255\|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	HIS225
B	HIS225
C	HIS225
D	HIS225

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255\|HAMAP-Rule:MF_00051

Chain	Residue	Details
A	LYS226
B	LYS226
C	LYS226
D	LYS226

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)