Structure of PDB 4n5n Chain B

Receptor sequence
>4n5nB (length=244) Species: 381666 (Cupriavidus necator H16) [Search protein sequence]
QRIAYVTGGMGGIGTAICQRLAKDGFRVVAGCGPNSPRREKWLEQQKALG
FDFIASEGNVADWDSTKTAFDKVKSEVGEVDVLINNAGITRDVVFRKMTR
ADWDAVIDTNLTSLFNVTKQVIDGMADRGWGRIVNISSVNGQKGQFGQTN
YSTAKAGLHGFTMALAQEVATKGVTVNTVSPGYIATDMVKAIRQDVLDKI
VATIPVKRLGLPEEIASICAWLSSEESGFSTGADFSLNGGLHMG
3D structure
PDB4n5n Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha
ChainB
Resolution1.9 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) 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 B G10 G13 G14 I15 G35 R40 G60 N61 V62 N88 S140 Y153 K157 P183 G184 G8 G11 G12 I13 G33 R38 G58 N59 V60 N86 S138 Y151 K155 P181 G182
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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Biological Process

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Cellular Component
External links
PDB RCSB:4n5n, PDBe:4n5n, PDBj:4n5n
PDBsum4n5n
PubMed24211201
UniProtP14697|PHAB_CUPNH Acetoacetyl-CoA reductase (Gene Name=phaB)

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