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Receptor Information

>2rhc Chain B (length=268) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

LVPRGSHMATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGL
RTTLKELREAGVEADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGR
PGGGATAELADELWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIA
STGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETP
MAASVREHYSDIWEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPG
AAAVTAQALNVCGGLGNY

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 B 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 G17 I18 R38 G39 C62 D63 V64 N90 S144 Y157 K161 P187 G188 V190 T192 M194
Binding residue (residue number reindexed from 1)	G20 T22 S23 G24 I25 R45 G46 C69 D70 V71 N97 S151 Y164 K168 P194 G195 V197 T199 M201
Annotation score	4

Catalytic site (original residue number in PDB)	G17 N114 S144 Y157 K161 Y202
Catalytic site (residue number reindexed from 1)	G24 N121 S151 Y164 K168 Y209
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 B Binding Site BS01