Structure of PDB 4xia Chain B

Receptor sequence

>4xiaB (length=393) Species: 1669 (Arthrobacter sp. NRRL B3728)

VQPTPADHFTFGLWTVGWTGADPFGVATRANLDPVEAVHKLAELGAYGIT
FHDNDLIPFDATAAEREKILGDFNQALADTGLKVPMVTTNLFSHPVFKDG
GFTSNDRSIRRFALAKVLHNIDLAAEMGAETFVMWGGREGSEYDGSKDLA
AALDRMREGVDTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF
IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLFHIDLNGQRGI
KYDQDLVFGHGDLTSAFFTVDLLENGFPNGGPKYTGPRHFDYKPSRTDGY
DGVWDSAKANMSMYLLLKERALAFRADPEVQEAMKTSGVFELGETTLNAG
ESAADLMNDSASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR

3D structure

• PDB: 4xia 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.
• Chain: B
• Resolution: 2.3 Å

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	SOR	B	H53 T89 V134 W136 E180 E216 H219 D292	H52 T88 V133 W135 E179 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

External links

• PDB: RCSB:4xia, PDBe:4xia, PDBj:4xia
• PDBsum: 4xia
• PubMed: 2769749
• UniProt: P12070|XYLA_ARTS7 Xylose isomerase (Gene Name=xylA)