Structure of PDB 3vzs Chain D

Receptor sequence
>3vzsD (length=249) Species: 381666 (Cupriavidus necator H16) [Search protein sequence]
HHGSTQRIAYVTGGMGGIGTAICQRLAKDGFRVVAGCGPNSPRREKWLEQ
QKALGFDFIASEGNVADWDSTKTAFDKVKSEVGEVDVLINNAGITRDVVF
RKMTRADWDAVIDTNLTSLFNVTKQVIDGMADRGWGRIVNISSVNGQKGQ
FGQTNYSTAKAGLHGFTMALAQEVATKGVTVNTVSPGYIATDMVKAIRQD
VLDKIVATIPVKRLGLPEEIASICAWLSSEESGFSTGADFSLNGGLHMG
3D structure
PDB3vzs Directed evolution and structural analysis of NADPH-dependent Acetoacetyl Coenzyme A (Acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics
ChainD
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N112 S140 Y153 K157
Catalytic site (residue number reindexed from 1) N115 S143 Y156 K160
Enzyme Commision number 1.1.1.36: acetoacetyl-CoA reductase.
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 I15 C34 G35 R40 G60 N61 V62 G90 I91 T92 P183 G184 I186 M190 V191 I18 C37 G38 R43 G63 N64 V65 G93 I94 T95 P186 G187 I189 M193 V194
BS02 CAA D D94 Q147 F148 Q150 Y153 G184 Y185 M190 D97 Q150 F151 Q153 Y156 G187 Y188 M193
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0018454 acetoacetyl-CoA reductase activity
Biological Process
GO:0042619 poly-hydroxybutyrate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3vzs, PDBe:3vzs, PDBj:3vzs
PDBsum3vzs
PubMed23913421
UniProtP14697|PHAB_CUPNH Acetoacetyl-CoA reductase (Gene Name=phaB)

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