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Receptor Information

>2rhc Chain A (length=257) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

DSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGLRTTLKELREAG
VEADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGRPGGGATAELAD
ELWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIASTGGKQGVVHA
APYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHYSD
IWEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPGAAAVTAQALNV
CGGLGNY

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

2rhc Chain A Residue 301 [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	2rhc Inhibition kinetics and emodin cocrystal structure of a type II polyketide ketoreductase
Resolution	2.1 Å
Binding residue (original residue number in PDB)	G13 T15 S16 I18 A37 R38 G39 C62 D63 V64 N90 G92 S144 Y157 K161 G188 V190 T192
Binding residue (residue number reindexed from 1)	G9 T11 S12 I14 A33 R34 G35 C58 D59 V60 N86 G88 S140 Y153 K157 G184 V186 T188
Annotation score	4

Catalytic site (original residue number in PDB)	G17 N114 S144 Y157 K161 Y202
Catalytic site (residue number reindexed from 1)	G13 N110 S140 Y153 K157 Y198
Enzyme Commision number	1.3.1.-

	Molecular Function
GO:0016491	oxidoreductase activity

	Biological Process
GO:0008202	steroid metabolic process
GO:0017000	antibiotic biosynthetic process

PDB	RCSB:2rhc, PDBe:2rhc, PDBj:2rhc
PDBsum	2rhc
PubMed	18205400
UniProt	P16544\|ACT3_STRCO Putative ketoacyl reductase (Gene Name=actIII)

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Structure of PDB 2rhc Chain A Binding Site BS01