Structure of PDB 4cqm Chain J Binding Site BS01

Receptor Information
>4cqm Chain J (length=240) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HHHMDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG
GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINRDGLLVRTKT
EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSV
YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKEEHLKKN
IPLGRFGETIEVAHAVVFLLESPYITGHVLVVDGGLQLIL
Ligand information
Ligand IDNAP
InChIInChI=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
InChIKeyXJLXINKUBYWONI-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(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 3.341NC(=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 3.341NC(=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 1.5.0c1cc(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
FormulaC21 H28 N7 O17 P3
NameNADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
ChEMBLCHEMBL295069
DrugBankDB03461
ZINC
PDB chain4cqm Chain J Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4cqm Insights Into Mitochondrial Fatty Acid Synthesis from the Structure of Heterotetrameric 3-Ketoacyl-Acp Reductase/3R-Hydroxyacyl-Coa Dehydrogenase.
Resolution2.339 Å
Binding residue
(original residue number in PDB)		G9 S11 R12 I14 A33 R34 D56 V57 A83 A84 G85 I86 V133 S135 Y148 K152 P178 V181 T183 M185
Binding residue
(residue number reindexed from 1)		G12 S14 R15 I17 A36 R37 D59 V60 A86 A87 G88 I89 V136 S138 Y151 K155 P181 V184 T186 M188
Annotation score4
Binding affinityMOAD: Kd=26.8uM
Enzymatic activity
Catalytic site (original residue number in PDB) G13 S135 Q145 Y148 K152
Catalytic site (residue number reindexed from 1) G16 S138 Q148 Y151 K155
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
1.6.5.10: NADPH dehydrogenase (quinone).
Gene Ontology
Molecular Function
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0005515 protein binding
GO:0008753 NADPH dehydrogenase (quinone) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0048038 quinone binding
GO:0070402 NADPH binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0044597 daunorubicin metabolic process
GO:0044598 doxorubicin metabolic process
GO:0046949 fatty-acyl-CoA biosynthetic process
GO:0051289 protein homotetramerization
GO:0051290 protein heterotetramerization
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:1990204 oxidoreductase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4cqm, PDBe:4cqm, PDBj:4cqm
PDBsum4cqm
PubMed25203508
UniProtQ8N4T8|CBR4_HUMAN 3-oxoacyl-[acyl-carrier-protein] reductase (Gene Name=CBR4)

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