Structure of PDB 9xim Chain C

Receptor sequence

>9ximC (length=391) Species: 1866 (Actinoplanes missouriensis)

QATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGITF
HDDDLVPFGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDGG
FTSNDRSVRRYAIRKVLRQMDLGAELGAKTLVLWGGREGAEYDSAKDVSA
ALDRYREALNLLAQYSEDRGYGLRFAIEPKPNQPRGDILLPTAGHAIAFV
QELERPELFGINPETGHEQMSNLNFTQGIAQALWHKKLFHIDLNGQHGPK
FDQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTEDYDG
VWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGEG
YAELLADRSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR

3D structure

• PDB: 9xim Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites.
• Chain: C
• 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): H51 D54 M85 E178 K180 E214 H217 D242 D252 D254 D289
• 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	C	H54 W137 E181 K183 H220 D292	H51 W134 E178 K180 H217 D289
BS02	MN	C	E181 E217 D245 D292	E178 E214 D242 D289
BS03	MN	C	E217 H220 D255 D257	E214 H217 D252 D254

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:9xim, PDBe:9xim, PDBj:9xim
• PDBsum: 9xim
• PubMed: 1610791
• UniProt: P12851|XYLA_ACTM4 Xylose isomerase (Gene Name=xylA)