Structure of PDB 2rh4 Chain B

Receptor sequence
>2rh4B (length=268) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
LVPRGSHMATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGL
RTTLKELREAGVEADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGR
PGGGATAELADELWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIA
STGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETP
MAASVREHYSDIWEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPG
AAAVTAQALNVCGGLGNY
3D structure
PDB2rh4 Inhibition kinetics and emodin cocrystal structure of a type II polyketide ketoreductase
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
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.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NDP B G13 T15 S16 I18 A37 R38 G39 C62 D63 V64 N90 S144 Y157 K161 G188 V190 T192 M194 G20 T22 S23 I25 A44 R45 G46 C69 D70 V71 N97 S151 Y164 K168 G195 V197 T199 M201
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
Biological Process
GO:0008202 steroid metabolic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2rh4, PDBe:2rh4, PDBj:2rh4
PDBsum2rh4
PubMed18205400
UniProtP16544|ACT3_STRCO Putative ketoacyl reductase (Gene Name=actIII)

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