Structure of PDB 1sm9 Chain A

Receptor sequence
>1sm9A (length=319) [Search protein sequence]
SIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYG
NEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADL
KVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKA
LEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKL
IEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYN
KTPAEVLLRWAAQRGIAVIPRSDLPERLVQNRSFNTFDLTKEDFEEIAKL
DIGLRFNDPWDWDNIPIFV
3D structure
PDB1sm9 The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.
ChainA
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 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 A G22 C23 W24 D47 Y52 H114 Q191 Y217 S218 F220 Q223 S224 E227 F240 A257 I272 R274 D276 R280 N284 G19 C20 W21 D44 Y49 H111 Q188 Y214 S215 F217 Q220 S221 E224 F237 A254 I269 R271 D273 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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Cellular Component
External links
PDB RCSB:1sm9, PDBe:1sm9, PDBj:1sm9
PDBsum1sm9
PubMed15320875
UniProtO74237|XYL1_CANTE NAD(P)H-dependent D-xylose reductase (Gene Name=XYL1)

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