Structure of PDB 1did Chain A

Receptor sequence

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

VQPTPADHFTFGLWTVGWTGADPFGVATRKNLDPVEAVHKLAELGAYGIT
FHDNDLIPFDATEAEREKILGDFNQALKDTGLKVPMVTTNLFSHPVFKDG
GFTSNDRSIRRFALAKVLHNIDLAAEMGAETFVMWGGREGSEYDGSKDLA
AALDRMREGVDTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF
IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLFHIDLNGQRGI
KYDQDLVFGHGDLTSAFFTVDLLENGFPNGGPKYTGPRHFDYKPSRTDGY
DGVWDSAKANMSMYLLLKERALAFRADPEVQEAMKTSGVFELGETTLNAG
ESAADLMNDSASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR

3D structure

• PDB: 1did Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase.
• 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	DIG	A	W15 H53 M87 W136 E180 D244 D292	W14 H52 M86 W135 E179 D243 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:1did, PDBe:1did, PDBj:1did
• PDBsum: 1did
• PubMed: 2304904
• UniProt: P12070|XYLA_ARTS7 Xylose isomerase (Gene Name=xylA)