Structure of PDB 1cyd Chain D

Receptor sequence
>1cydD (length=242) Species: 10090 (Mus musculus) [Search protein sequence]
LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKECP
GIEPVCVDLGDWDATEKALGGIGPVDLLVNNAALVIMQPFLEVTKEAFDR
SFSVNLRSVFQVSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSST
KGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKE
RHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS
3D structure
PDB1cyd Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family.
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) G18 S136 L146 Y149 K153
Catalytic site (residue number reindexed from 1) G16 S134 L144 Y147 K151
Enzyme Commision number 1.1.1.184: carbonyl reductase (NADPH).
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 NDP D G14 G16 K17 I19 T38 R39 T40 L61 N83 A85 V106 V134 S136 Y149 K153 P179 V181 V182 T184 M186 G187 G12 G14 K15 I17 T36 R37 T38 L59 N81 A83 V104 V132 S134 Y147 K151 P177 V179 V180 T182 M184 G185
BS02 IPA D S136 Y149 S134 Y147
Gene Ontology
Molecular Function
GO:0004090 carbonyl reductase (NADPH) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006116 NADH oxidation
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Cellular Component
External links
PDB RCSB:1cyd, PDBe:1cyd, PDBj:1cyd
PDBsum1cyd
PubMed8805511
UniProtP08074|CBR2_MOUSE Carbonyl reductase [NADPH] 2 (Gene Name=Cbr2)

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