Structure of PDB 1mi3 Chain D

Receptor sequence
>1mi3D (length=319) [Search protein sequence]
SIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYG
NEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADL
KVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKA
LEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKL
IEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYN
KTPAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKL
DIGLRFNDPWDWDNIPIFV
3D structure
PDB1mi3 Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases
ChainD
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D G22 C23 W24 D47 Y52 N170 Q191 Y217 S218 F220 Q223 S224 E227 F240 A257 I272 P273 K274 N276 R280 N284 N310 G19 C20 W21 D44 Y49 N167 Q188 Y214 S215 F217 Q220 S221 E224 F237 A254 I269 P270 K271 N273 R277 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

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Cellular Component
External links
PDB RCSB:1mi3, PDBe:1mi3, PDBj:1mi3
PDBsum1mi3
PubMed12733986
UniProtO74237|XYL1_CANTE NAD(P)H-dependent D-xylose reductase (Gene Name=XYL1)

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