Structure of PDB 3gp3 Chain A

Receptor sequence
>3gp3A (length=229) Species: 28450 (Burkholderia pseudomallei) [Search protein sequence]
MYKLVLIRHGESTWNKENRFTGWVDVDLTEQGNREARQAGQLLKEAGYTF
DIAYTSVLKRAIRTLWHVQDQMDLMYVPVVHSWRLNERHYGALSGLNKAE
TAAKYGDEQVLVWRRSYDTPPPALEPGDERAPYADPRYAKVPREQLPLTE
CLKDTVARVLPLWNESIAPAVKAGKQVLIAAHGNSLRALIKYLDGISDAD
IVGLNIPNGVPLVYELDESLTPIRHYYLG
3D structure
PDB3gp3 An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H9 R60 E87 H182
Catalytic site (residue number reindexed from 1) H9 R60 E87 H182
Enzyme Commision number 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PO3 A R8 H9 R60 E87 H182 G183 R8 H9 R60 E87 H182 G183
BS02 SEP A T21 E87 Y90 K98 R114 R115 N184 T21 E87 Y90 K98 R114 R115 N184
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004619 phosphoglycerate mutase activity
GO:0016853 isomerase activity
GO:0016868 intramolecular phosphotransferase activity
GO:0046538 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gp3, PDBe:3gp3, PDBj:3gp3
PDBsum3gp3
PubMed21904048
UniProtQ3JWH7|GPMA_BURP1 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (Gene Name=gpmA)

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