Structure of PDB 4c4r Chain A

Receptor sequence
>4c4rA (length=218) Species: 1358 (Lactococcus lactis) [Search protein sequence]
MFKAVLFDLDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSRE
DSLQKILDLADKKVSAEEFKELAKRKNDNYVKMIQDVSPADVYPGILQLL
KDLRSNKIKIALASASKNGPFLLERMNLTGYFDAIADPAEVAASKPAPDI
FIAAAHAVGVAPSESIGLEDSQAGIQAIKDSGALPIGVGRPEDLGDDIVI
VPDTSHYTLEFLKEVWLQ
3D structure
PDB4c4r Alpha-Fluorophosphonates Reveal How a Phosphomutase Conserves Transition State Conformation Over Hexose Recognition in its Two-Step Reaction.
ChainA
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D8 L9 D10 T16 K45 S114 A115 K145 E169 D170
Catalytic site (residue number reindexed from 1) D8 L9 D10 T16 K45 S114 A115 K145 E169 D170
Enzyme Commision number 5.4.2.6: beta-phosphoglucomutase.
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 MG A D8 D10 D170 D8 D10 D170
BS02 YO5 A D10 H20 W24 L44 G46 V47 R49 S52 S116 K117 D10 H20 W24 L44 G46 V47 R49 S52 S116 K117 MOAD: Kd=1.3mM
BS03 MGF A D8 L9 D10 S114 A115 K145 D8 L9 D10 S114 A115 K145
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008801 beta-phosphoglucomutase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:4c4r, PDBe:4c4r, PDBj:4c4r
PDBsum4c4r
PubMed25104750
UniProtP71447|PGMB_LACLA Beta-phosphoglucomutase (Gene Name=pgmB)

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