Structure of PDB 1x83 Chain B Binding Site BS01
Receptor Information
>1x83 Chain B (length=180) Species:
562
(Escherichia coli) [
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EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRAL
SKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFR
FRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDA
TPWAFSPWMVMQATNREARKRLSAFTQLKL
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1x83 Chain B Residue 201 [
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Receptor-Ligand Complex Structure
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PDB
1x83
A Crystallographic Investigation of Phosphoantigen Binding to Isopentenyl Pyrophosphate/Dimethylallyl Pyrophosphate Isomerase
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
H25 H32 H69 E114 E116
Binding residue
(residue number reindexed from 1)
H22 H29 H66 E111 E113
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H25 H32 C67 H69 E87 F104 E114 E116 W161
Catalytic site (residue number reindexed from 1)
H22 H29 C64 H66 E84 F101 E111 E113 W158
Enzyme Commision number
5.3.3.2
: isopentenyl-diphosphate Delta-isomerase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0003824
catalytic activity
GO:0004452
isopentenyl-diphosphate delta-isomerase activity
GO:0008270
zinc ion binding
GO:0016853
isomerase activity
GO:0046872
metal ion binding
Biological Process
GO:0006974
DNA damage response
GO:0008299
isoprenoid biosynthetic process
GO:0050992
dimethylallyl diphosphate biosynthetic process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1x83
,
PDBe:1x83
,
PDBj:1x83
PDBsum
1x83
PubMed
15643873
UniProt
Q46822
|IDI_ECOLI Isopentenyl-diphosphate Delta-isomerase (Gene Name=idi)
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