Structure of PDB 1xyc Chain A

Receptor sequence

>1xycA (length=386) Species: 1963 (Streptomyces olivochromogenes)

SYQPTPEDRFTFGLWTVGWQGRDPFGDATRPALDPVETVQRLAELGAHGV
TFHDDDLIPFGSSDTERESHIKRFRQALDATGMTVPMATTNLFTHPVFKD
GGFTANDRDVRRYALRKTIRNIDLAVELGAKTYVAWGGREGAESGAAKDV
RVALDRMKEAFDLLGEYVTSQGYDTRFAIEPKPNEPRGDILLPTVGHALA
FIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSG
IKYDQDLRFGAGDLRAAFWLVDLLESAGYEGPRHFDFKPPRTEDIDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELAQPTAADGVQELL
ADRTAFEDFDVDAAAARGMAFERLDQLAMDHLLGAR

3D structure

• PDB: 1xyc X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
• Chain: A
• Resolution: 2.19 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M87
• Catalytic site (residue number reindexed from 1): M87
• 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	3MF	A	W15 H53 T89 W136 E180 K182 H219 D286	W15 H53 T89 W136 E180 K182 H219 D286
BS02	MG	A	E180 E216 D244 D286	E180 E216 D244 D286
BS03	MG	A	E216 H219 D254 D256	E216 H219 D254 D256

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:1xyc, PDBe:1xyc, PDBj:1xyc
• PDBsum: 1xyc
• PubMed: 8180169
• UniProt: P15587|XYLA_STROL Xylose isomerase (Gene Name=xylA)