Structure of PDB 5xia Chain B

Receptor sequence
>5xiaB (length=393) Species: 1669 (Arthrobacter sp. NRRL B3728) [Search protein sequence]
VQPTPADHFTFGLWTVGWTGADPFGVATRANLDPVEAVHKLAELGAYGIT
FHDNDLIPFDATAAEREKILGDFNQALADTGLKVPMVTTNLFSHPVFKDG
GFTSNDRSIRRFALAKVLHNIDLAAEMGAETFVMWGGREGSEYDGSKDLA
AALDRMREGVDTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF
IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLFHIDLNGQRGI
KYDQDLVFGHGDLTSAFFTVDLLENGFPNGGPKYTGPRHFDYKPSRTDGY
DGVWDSAKANMSMYLLLKERALAFRADPEVQEAMKTSGVFELGETTLNAG
ESAADLMNDSASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR
3D structure
PDB5xia Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A resolution, respectively.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 XYL B H53 W136 E180 K182 E216 H219 D292 H52 W135 E179 K181 E215 H218 D291
BS02 MG B E180 E216 D244 D292 E179 E215 D243 D291
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:5xia, PDBe:5xia, PDBj:5xia
PDBsum5xia
PubMed2769749
UniProtP12070|XYLA_ARTS7 Xylose isomerase (Gene Name=xylA)

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