Structure of PDB 3ri3 Chain B

Receptor sequence

>3ri3B (length=257) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]

RGSHMATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGLRTT
LKELREAGVEADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGRLGG
GATAELADELWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIASTG
GKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAA
SVREHTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPGAAAVTAQALNV
CGGLGNY

3D structure

PDB

3ri3 Structural and Biochemical Analyses of Regio- and Stereospecificities Observed in a Type II Polyketide Ketoreductase.

Chain

Resolution

2.292 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
Catalytic site (residue number reindexed from 1)	G21 N118 S148 Y161 K165
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	B	G13 T15 S16 I18 R38 G39 C62 V64 N90 A91 S144 Y157 K161 P187 G188 V190 T192 P193 M194	G17 T19 S20 I22 R42 G43 C66 V68 N94 A95 S148 Y161 K165 P191 G192 V194 T196 P197 M198
BS02	EMO	B	V151 V198 L258	V155 V202 L254
BS03	EMO	B	S144 Y157 G188 F189 M194 V198 I217 L258	S148 Y161 G192 F193 M198 V202 I213 L254

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

View graph for
Biological Process

External links

PDB	RCSB:3ri3, PDBe:3ri3, PDBj:3ri3
PDBsum	3ri3
PubMed	21506596
UniProt	P16544\|ACT3_STRCO Putative ketoacyl reductase (Gene Name=actIII)

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