Structure of PDB 4cqm Chain I Binding Site BS01

Receptor Information
>4cqm Chain I (length=249) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLQNRLRSALALVTGAGSGIGRAVSVRLAGEGATVAACDLDRAAAQETVR
LLPRGNHAAFQADVSEARAARCLLEQVQACFSRPPSVVVSCAGITQDEFL
LHMSEDDWDKVIAVNLKGTFLVTQAAAQALVSNGCRGSIINISSIVGKVG
NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKVPQ
KVVDKITEMIPMGHLGDPEDVADVVAFLASEDSGYITGTSVEVTGGLFM
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 I 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)		G18 S21 G22 I23 D42 L43 A74 D75 V76 C103 A104 G105 I106 V126 I154 S156 Y169 K173 P199 G200 T204 P205 M206
Binding residue
(residue number reindexed from 1)		G15 S18 G19 I20 D39 L40 A62 D63 V64 C91 A92 G93 I94 V114 I142 S144 Y157 K161 P187 G188 T192 P193 M194
Annotation score3
Binding affinityMOAD: Kd=26.8uM
Enzymatic activity
Catalytic site (original residue number in PDB) G22 S156 Y169 K173
Catalytic site (residue number reindexed from 1) G19 S144 Y157 K161
Enzyme Commision number 1.1.1.239: 3alpha-(17beta)-hydroxysteroid dehydrogenase (NAD(+)).
1.1.1.62: 17beta-estradiol 17-dehydrogenase.
1.1.1.n12: (3R)-hydroxyacyl-CoA dehydrogenase.
Gene Ontology
Molecular Function
GO:0004303 estradiol 17-beta-dehydrogenase [NAD(P)+] activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0047035 testosterone dehydrogenase (NAD+) activity
GO:0070404 NADH binding
GO:0106386 (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0006694 steroid biosynthetic process
GO:0006703 estrogen biosynthetic process
GO:0008209 androgen metabolic process
GO:0008210 estrogen metabolic process
GO:0051290 protein heterotetramerization
Cellular Component
GO:0005739 mitochondrion
GO:0005740 mitochondrial envelope
GO:0005759 mitochondrial matrix
GO:0005886 plasma membrane
GO:0016020 membrane
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
UniProtQ92506|DHB8_HUMAN (3R)-3-hydroxyacyl-CoA dehydrogenase (Gene Name=HSD17B8)

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