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Receptor Information

>3vzs Chain D (length=249) Species: 381666 (Cupriavidus necator H16) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

HHGSTQRIAYVTGGMGGIGTAICQRLAKDGFRVVAGCGPNSPRREKWLEQ
QKALGFDFIASEGNVADWDSTKTAFDKVKSEVGEVDVLINNAGITRDVVF
RKMTRADWDAVIDTNLTSLFNVTKQVIDGMADRGWGRIVNISSVNGQKGQ
FGQTNYSTAKAGLHGFTMALAQEVATKGVTVNTVSPGYIATDMVKAIRQD
VLDKIVATIPVKRLGLPEEIASICAWLSSEESGFSTGADFSLNGGLHMG

Ligand ID

NAP

InChI

InChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

InChIKey

XJLXINKUBYWONI-NNYOXOHSSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N

Formula

C21 H28 N7 O17 P3

Name

NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE

PDB chain

3vzs Chain D Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	3vzs Directed evolution and structural analysis of NADPH-dependent Acetoacetyl Coenzyme A (Acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics
Resolution	2.14 Å
Binding residue (original residue number in PDB)	I15 C34 G35 R40 G60 N61 V62 G90 I91 T92 P183 G184 I186 M190 V191
Binding residue (residue number reindexed from 1)	I18 C37 G38 R43 G63 N64 V65 G93 I94 T95 P186 G187 I189 M193 V194
Annotation score	4

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.

	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

PDB	RCSB:3vzs, PDBe:3vzs, PDBj:3vzs
PDBsum	3vzs
PubMed	23913421
UniProt	P14697\|PHAB_CUPNH Acetoacetyl-CoA reductase (Gene Name=phaB)

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Structure of PDB 3vzs Chain D Binding Site BS01