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Receptor Information

>1w4z Chain B (length=261) Species: 1902 (Streptomyces coelicolor) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

LVPRGSHMATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGL
RTTLKELREAGVEADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGR
PGGGATAELADELWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIA
STGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETP
MAASVREHYTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPGAAAVTAQ
ALNVCGGLGNY

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

1w4z Chain B Residue 1262 [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	1w4z The Crystal Structure of the Actiii Actinorhodin Polyketide Reductase; Proposed Mechanism for Acp and Polyketide Binding
Resolution	2.5 Å
Binding residue (original residue number in PDB)	G13 T15 S16 I18 R38 G39 D63 V64 N90 A91 G92 S144 Y157 K161 P187 G188 V190 T192 M194
Binding residue (residue number reindexed from 1)	G20 T22 S23 I25 R45 G46 D70 V71 N97 A98 G99 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:1w4z, PDBe:1w4z, PDBj:1w4z
PDBsum	1w4z
PubMed	15458634
UniProt	P16544\|ACT3_STRCO Putative ketoacyl reductase (Gene Name=actIII)

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Structure of PDB 1w4z Chain B Binding Site BS01