Structure of PDB 3ri3 Chain A

Receptor sequence
>3ri3A (length=256) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
SEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGLRTTLKELREAGV
EADGRTCDVRSVPEIEALVAAVVERYGPVDVLVNNAGRLGGGATAELADE
LWLDVVETNLTGVFRVTKQVLKAGGMLERGTGRIVNIASTGGKQGVVHAA
PYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHYSDI
WEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLIGPGAAAVTAQALNVC
GGLGNY
3D structure
PDB3ri3 Structural and Biochemical Analyses of Regio- and Stereospecificities Observed in a Type II Polyketide Ketoreductase.
ChainA
Resolution2.292 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 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)		 Binding affinity
BS01 NDP A G13 T15 S16 G17 I18 A37 R38 G39 C62 D63 V64 N90 A91 S144 Y157 K161 P187 G188 V190 T192 M194 G8 T10 S11 G12 I13 A32 R33 G34 C57 D58 V59 N85 A86 S139 Y152 K156 P182 G183 V185 T187 M189
BS02 EMO A S144 Y157 G188 F189 S139 Y152 G183 F184
BS03 EMO A T145 Q149 V151 T140 Q144 V146
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:3ri3, PDBe:3ri3, PDBj:3ri3
PDBsum3ri3
PubMed21506596
UniProtP16544|ACT3_STRCO Putative ketoacyl reductase (Gene Name=actIII)

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