Structure of PDB 1did Chain A Binding Site BS03
Receptor Information
>1did Chain A (length=393) Species:
1669
(Arthrobacter sp. NRRL B3728) [
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VQPTPADHFTFGLWTVGWTGADPFGVATRKNLDPVEAVHKLAELGAYGIT
FHDNDLIPFDATEAEREKILGDFNQALKDTGLKVPMVTTNLFSHPVFKDG
GFTSNDRSIRRFALAKVLHNIDLAAEMGAETFVMWGGREGSEYDGSKDLA
AALDRMREGVDTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF
IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLFHIDLNGQRGI
KYDQDLVFGHGDLTSAFFTVDLLENGFPNGGPKYTGPRHFDYKPSRTDGY
DGVWDSAKANMSMYLLLKERALAFRADPEVQEAMKTSGVFELGETTLNAG
ESAADLMNDSASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR
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
1did Chain A Residue 399 [
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Receptor-Ligand Complex Structure
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PDB
1did
Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
E180 E216 D244 D292
Binding residue
(residue number reindexed from 1)
E179 E215 D243 D291
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H53 D56 M87 E180 K182 E216 H219 D244 D254 D256 D292
Catalytic site (residue number reindexed from 1)
H52 D55 M86 E179 K181 E215 H218 D243 D253 D255 D291
Enzyme Commision number
5.3.1.5
: xylose isomerase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0009045
xylose isomerase activity
GO:0016853
isomerase activity
GO:0046872
metal ion binding
Biological Process
GO:0005975
carbohydrate metabolic process
GO:0042732
D-xylose metabolic 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:1did
,
PDBe:1did
,
PDBj:1did
PDBsum
1did
PubMed
2304904
UniProt
P12070
|XYLA_ARTS7 Xylose isomerase (Gene Name=xylA)
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