1EQJ

CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006007	biological_process	glucose catabolic process
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0030145	molecular_function	manganese ion binding
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
A	0043937	biological_process	regulation of sporulation
A	0046537	molecular_function	2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 601

Chain	Residue
A	ASP403
A	HIS407
A	ASN447
A	HIS462
A	2PG801

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 701

Chain	Residue
A	2PG801
A	ASP12
A	SER62
A	ASP444
A	HIS445

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site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 2PG A 801

Chain	Residue
A	ASN61
A	SER62
A	HIS123
A	ARG153
A	ASP154
A	ARG185
A	ARG191
A	ARG261
A	ARG264
A	LYS336
A	ASP403
A	HIS407
A	HIS445
A	HIS462
A	MN601
A	MN701
A	HOH963

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:10747010, ECO:0000269|PubMed:10764795, ECO:0000269|PubMed:12729763

Chain	Residue	Details
A	SER62

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:10747010, ECO:0000269|PubMed:10764795

Chain	Residue	Details
A	ASP12
A	SER62
A	ARG191
A	ASP444
A	HIS445

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:10747010, ECO:0000269|PubMed:10764795, ECO:0000269|PubMed:12729763

Chain	Residue	Details
A	HIS123
A	ARG153
A	ARG185
A	ARG261
A	ASP403
A	HIS407
A	HIS462

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:10747010, ECO:0000269|PubMed:12729763

Chain	Residue	Details
A	LYS336

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_01038

Chain	Residue	Details
A	TYR36

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1o98

Chain	Residue	Details
A	SER62
A	ASP154
A	ARG261

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site_id	MCSA1
Number of Residues	10
Details	M-CSA 738

Chain	Residue	Details
A	ASP12	metal ligand
A	HIS462	metal ligand
A	SER62	metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
A	ASP154	proton acceptor, proton donor
A	ARG261	electrostatic stabiliser
A	LYS336	proton acceptor, proton donor
A	ASP403	metal ligand
A	HIS407	metal ligand
A	ASP444	metal ligand
A	HIS445	metal ligand

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