Structure of PDB 1xim Chain A

Receptor sequence

>1ximA (length=392) Species: 1866 (Actinoplanes missouriensis)

VQATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGIT
FHDDDLVPFGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDG
GFTSNDRSVRRYAIRKVLRQMDLGAELGAKTLVLWGGREGAEYDSAKDVS
AALDRYREALNLLAQYSEDRGYGLRFAIEPKPNEPRGDILLPTAGHAIAF
VQELERPELFGINPETGHEQMSNLNFTQGIAQALWHKKLFHIDLNGQHGP
KFDQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTEDYD
GVWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGE
GYAELLADRSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR

3D structure

• PDB: 1xim Arginine residues as stabilizing elements in proteins.
• Chain: A
• Resolution: 2.2 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	XYL	A	H54 W137 E181 K183 H220 D292	H52 W135 E179 K181 H218 D290
BS02	CO	A	E181 E217 D245 D292	E179 E215 D243 D290
BS03	CO	A	E217 H220 D255 D257	E215 H218 D253 D255

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:1xim, PDBe:1xim, PDBj:1xim
• PDBsum: 1xim
• PubMed: 1540579
• UniProt: P12851|XYLA_ACTM4 Xylose isomerase (Gene Name=xylA)