Structure of PDB 1r38 Chain D

Receptor sequence
>1r38D (length=319) [Search protein sequence]
SIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYG
NEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADL
KVDYVDLFLIAFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKA
LEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKL
IEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYN
KTPAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKL
DIGLRFNDPWDWDNIPIFV
3D structure
PDB1r38 Studies of the enzymic mechanism of Candida tenuis xylose reductase (AKR 2B5): X-ray structure and catalytic reaction profile for the H113A mutant
ChainD
Resolution2.2 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 A114
Catalytic site (residue number reindexed from 1) D44 Y49 K78 A111
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 NAP D G22 C23 W24 D47 Y52 S169 N170 Q191 Y217 S218 F220 Q223 S224 F240 A257 I272 K274 S275 N276 R280 N284 G19 C20 W21 D44 Y49 S166 N167 Q188 Y214 S215 F217 Q220 S221 F237 A254 I269 K271 S272 N273 R277 N281
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1r38, PDBe:1r38, PDBj:1r38
PDBsum1r38
PubMed15109252
UniProtO74237|XYL1_CANTE NAD(P)H-dependent D-xylose reductase (Gene Name=XYL1)

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