Structure of PDB 1oad Chain A

Receptor sequence

>1oadA (length=387) Species: 1929 (Streptomyces rubiginosus)

NYQPTPEDRFTFGLWTVGWEGRDPFGDATRRALDPVESVRRLAELGAHGV
TFHDDDLIPFGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFKD
GGFTANDRDVRRYALRKTIRNIDLAVELGAETYVAWGGREGAESGGAKDV
RDALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTVGHALA
FIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQNG
IKYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQALL
DDRSAFEEFDVDAAAARGMAFERLDQLAMDHLLGARG

3D structure

• PDB: 1oad Sad Manganese in Two Crystal Forms of Glucose Isomerase
• Chain: A
• Resolution: 1.5 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): H53 D56 M87 E180 K182 E216 H219 D244 D254 D256 D286
• 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	MN	A	E217 H220 D255 D257	E216 H219 D254 D256
BS02	MG	A	E181 E217 D245 D287	E180 E216 D244 D286
BS03	MQD	A	W16 H54 F94 W137 E181 D287	W15 H53 F93 W136 E180 D286

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:1oad, PDBe:1oad, PDBj:1oad
• PDBsum: 1oad
• PubMed: 12777803
• UniProt: P24300|XYLA_STRRU Xylose isomerase (Gene Name=xylA)