Structure of PDB 1bq3 Chain D

Receptor sequence
>1bq3D (length=234) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPD
VLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAET
LKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETES
LALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADI
AKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAA
3D structure
PDB1bq3 Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis.
ChainD
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H8 R59 E86 H181
Catalytic site (residue number reindexed from 1) H8 R59 E86 H181
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 IHP D R7 S11 W13 N14 L18 F19 T20 K97 R113 R7 S11 W13 N14 L18 F19 T20 K97 R113 PDBbind-CN: -logKd/Ki=5.40,Ki=4uM
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
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane
GO:0005758 mitochondrial intermembrane space
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1bq3, PDBe:1bq3, PDBj:1bq3
PDBsum1bq3
PubMed10369755
UniProtP00950|PMG1_YEAST Phosphoglycerate mutase 1 (Gene Name=GPM1)

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