Structure of PDB 1xih Chain A

Receptor sequence

>1xihA (length=385) Species: 1929 (Streptomyces rubiginosus)

YQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVESVQRLAELGAHGVT
FHDDDLIPFGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFKDG
GFTANDRDVRRYALRKTIRNIDLAVELGAETYVAWGGREGAESGGAKDVR
DALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTVGHALAF
IERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQNGI
KYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVWAS
AAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQALLD
DRSAFEEFDVDAAAARGMAFERLDQLAMDHLLGAR

3D structure

• PDB: 1xih Modes of binding substrates and their analogues to the enzyme D-xylose isomerase.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H54 D57 M88 E181 K183 E217 H220 D245 D255 D257 D287
• Catalytic site (residue number reindexed from 1): H52 D55 M86 E179 K181 E215 H218 D243 D253 D255 D285
• 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	SOR	A	H54 T90 V135 W137 E181 K183 E217 H220 D287	H52 T88 V133 W135 E179 K181 E215 H218 D285
BS02	MN	A	E181 E217 D245 D287	E179 E215 D243 D285

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0009045 xylose isomerase activity
• GO:0016853 isomerase activity
• GO:0042802 identical protein binding
• 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:1xih, PDBe:1xih, PDBj:1xih
• PDBsum: 1xih
• PubMed: 15299449
• UniProt: P24300|XYLA_STRRU Xylose isomerase (Gene Name=xylA)