Structure of PDB 3vzs Chain C

Receptor sequence
>3vzsC (length=244) Species: 381666 (Cupriavidus necator H16) [Search protein sequence]
QRIAYVTGGMGGIGTAICQRLAKDGFRVVAGCGPNSPRREKWLEQQKALG
FDFIASEGNVADWDSTKTAFDKVKSEVGEVDVLINNAGITRDVVFRKMTR
ADWDAVIDTNLTSLFNVTKQVIDGMADRGWGRIVNISSVNGQKGQFGQTN
YSTAKAGLHGFTMALAQEVATKGVTVNTVSPGYIATDMVKAIRQDVLDKI
VATIPVKRLGLPEEIASICAWLSSEESGFSTGADFSLNGGLHMG
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
ChainC
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N112 S140 Y153 K157
Catalytic site (residue number reindexed from 1) N110 S138 Y151 K155
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 C G10 I15 G35 R40 G60 N61 V62 G90 I91 T92 T111 P183 G184 I186 T188 M190 V191 G8 I13 G33 R38 G58 N59 V60 G88 I89 T90 T109 P181 G182 I184 T186 M188 V189
BS02 CAA C D94 Q147 F148 Q150 Y153 G184 Y185 M190 R195 D92 Q145 F146 Q148 Y151 G182 Y183 M188 R193
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

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

[Back to BioLiP]