Structure of PDB 8xim Chain A

Receptor sequence

>8ximA (length=392) Species: 1866 (Actinoplanes missouriensis)

VQATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGIT
FHDDDLVPFGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDG
GFTSNDRSVRRYAIRKVLRQMDLGAELGAKTLVLWGGREGAEYDSAKDVS
AALDRYREALNLLAQYSEDRGYGLRFAIEPKPNQPRGDILLPTAGHAIAF
VQELERPELFGINPETGHEQMSNLNFTQGIAQALWHKKLFHIDLNGQHGP
KFDQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTEDYD
GVWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGE
GYAELLADRSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR

3D structure

• PDB: 8xim Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H54 D57 M88 E181 K183 E217 H220 D245 D255 D257 D292
• Catalytic site (residue number reindexed from 1): H52 D55 M86 E179 K181 E215 H218 D243 D253 D255 D290
• 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	XLS	A	H54 W137 E181 K183 E217 H220 D292	H52 W135 E179 K181 E215 H218 D290
BS02	MG	A	E181 E217 D245 D292	E179 E215 D243 D290

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:8xim, PDBe:8xim, PDBj:8xim
• PDBsum: 8xim
• PubMed: 1610791
• UniProt: P12851|XYLA_ACTM4 Xylose isomerase (Gene Name=xylA)