Structure of PDB 2rhr Chain A

Receptor sequence

>2rhrA (length=256) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]

SEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGLRTTLKELREAGV
EADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGRLGGGATAELADE
LWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIASTGGKQGVVHAA
PYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHYSDI
WEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPGAAAVTAQALNVC
GGLGNY

3D structure

PDB

2rhr Inhibition kinetics and emodin cocrystal structure of a type II polyketide ketoreductase

Chain

Resolution

2.5 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	G17 N114 S144 Y157 K161 Y202
Catalytic site (residue number reindexed from 1)	G12 N109 S139 Y152 K156 Y197
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)
BS01	NDP	A	G13 T15 S16 G17 I18 R38 G39 C62 D63 V64 N90 A91 G92 I142 Y157 K161 P187 F189 V190 T192 M194	G8 T10 S11 G12 I13 R33 G34 C57 D58 V59 N85 A86 G87 I137 Y152 K156 P182 F184 V185 T187 M189
BS02	EMO	A	Y157 G188 F189 V198 I217 L258	Y152 G183 F184 V193 I212 L253
BS03	EMO	A	T145 Q149 V151 R220 L258	T140 Q144 V146 R215 L253

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity

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

View graph for
Molecular Function

View graph for
Biological Process

External links

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

[Back to BioLiP]