Structure of PDB 1xld Chain A

Receptor sequence

>1xldA (length=393) Species: 1669 (Arthrobacter sp. NRRL B3728)

VQPTPADHFTFGLWTVGWTGADPFGVATRKNLDPVEAVHKLAELGAYGIT
FHDNDLIPFDATEAEREKILGDFNQALKDTGLKVPMVTTNLFSHPVFKDG
GFTSNDRSIRRFALAKVLHNIDLAAEMGAETFVMWGGREGSEYDGSKDLA
AALDRMREGVDTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF
IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLFHIDLNGQRGI
KYDQDLVFGHGDLTSAFFTVDLLENGFPNGGPKYTGPRHFDYKPSRTDGY
DGVWDSAKANMSMYLLLKERALAFRADPEVQEAMKTSGVFELGETTLNAG
ESAADLMNDSASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR

3D structure

• PDB: 1xld Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift.
• Chain: A
• Resolution: 2.5 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	XYL	A	H53 W136 E180 H219 D292	H52 W135 E179 H218 D291
BS02	MN	A	E216 H219 D254 D256	E215 H218 D253 D255
BS03	MN	A	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:1xld, PDBe:1xld, PDBj:1xld
• PDBsum: 1xld
• PubMed: 2319597
• UniProt: P12070|XYLA_ARTS7 Xylose isomerase (Gene Name=xylA)