Structure of PDB 4cql Chain E Binding Site BS01

Receptor Information
>4cql Chain E (length=244) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QNRLRSALALVTGAGSGIGRAVSVRLAGEGATVAACDLDRAAAQETVRLL
NHAAFQADVSEARAARCLLEQVQACFSRPPSVVVSCAGITQDEFLLHMSE
DDWDKVIAVNLKGTFLVTQAAAQALVSNGCRGSIINISSIVGKVGNVGQT
NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKVPQKVVDK
ITEMIPMGHLGDPEDVADVVAFLASEDSGYITGTSVEVTGGLFM
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
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)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)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)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]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)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain4cql Chain E Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4cql Insights Into Mitochondrial Fatty Acid Synthesis from the Structure of Heterotetrameric 3-Ketoacyl-Acp Reductase/3R-Hydroxyacyl-Coa Dehydrogenase.
Resolution2.85 Å
Binding residue
(original residue number in PDB)		S21 G22 I23 D42 L43 A74 D75 V76 C103 A104 G105 I106 V126 I154 S156 Y169 K173 T204 M206
Binding residue
(residue number reindexed from 1)		S16 G17 I18 D37 L38 A57 D58 V59 C86 A87 G88 I89 V109 I137 S139 Y152 K156 T187 M189
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) G22 S156 Y169 K173
Catalytic site (residue number reindexed from 1) G17 S139 Y152 K156
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:4cql, PDBe:4cql, PDBj:4cql
PDBsum4cql
PubMed25203508
UniProtQ92506|DHB8_HUMAN (3R)-3-hydroxyacyl-CoA dehydrogenase (Gene Name=HSD17B8)

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