Structure of PDB 6hdj Chain A

Receptor sequence
>6hdjA (length=219) Species: 272623 (Lactococcus lactis subsp. lactis Il1403) [Search protein sequence]
MFKAVLFDLDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSKE
DSLQKILDLADKKVSAEEFKELAKRKNDNYVKMIQDVSPADVYPGILQLL
KDLRSNKIKIALASASKNGPFLLERMNLTGYFDAIADPAEVAASKPAPDI
FIAAAHAVGVAPSESIGLEDSQAGIQAIKDSGALPIGVGRPEDLGDDIVI
VPDTSHYTLEFLKEVWLQK
3D structure
PDB6hdj Transition state of phospho-enzyme hydrolysis in beta-phosphoglucomutase.
ChainA
Resolution1.16 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ALF A D8 L9 D10 S114 K145 D8 L9 D10 S114 K145
BS03 BG6 A D10 H20 G46 V47 K49 S116 K117 D10 H20 G46 V47 K49 S116 K117
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6hdj, PDBe:6hdj, PDBj:6hdj
PDBsum6hdj
PubMed
UniProtP71447|PGMB_LACLA Beta-phosphoglucomutase (Gene Name=pgmB)

[Back to BioLiP]