Structure of PDB 1mi3 Chain C

Receptor sequence

>1mi3C (length=319)

SIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYG
NEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADL
KVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKA
LEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKL
IEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYN
KTPAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKL
DIGLRFNDPWDWDNIPIFV

3D structure

• PDB: 1mi3 Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases
• Chain: C
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D47 Y52 K81 H114
• Catalytic site (residue number reindexed from 1): D44 Y49 K78 H111
• Enzyme Commision number: 1.1.1.307: D-xylose reductase [NAD(P)H].

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	NAD	C	G22 C23 W24 D47 Y52 H114 N170 Q191 Y217 S218 F220 Q223 S224 E227 A257 I272 P273 K274 N276 R280 Q283 N284 N310	G19 C20 W21 D44 Y49 H111 N167 Q188 Y214 S215 F217 Q220 S221 E224 A254 I269 P270 K271 N273 R277 Q280 N281 N307

Gene Ontology

Molecular Function

• GO:0004032 aldose reductase (NADPH) activity
• GO:0016491 oxidoreductase activity
• GO:0032866 D-xylose reductase (NADPH) activity

Biological Process

• GO:0042732 D-xylose metabolic process
• GO:0042843 D-xylose catabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1mi3, PDBe:1mi3, PDBj:1mi3
• PDBsum: 1mi3
• PubMed: 12733986
• UniProt: O74237|XYL1_CANTE NAD(P)H-dependent D-xylose reductase (Gene Name=XYL1)