Structure of PDB 3v0t Chain A

Receptor sequence
>3v0tA (length=287) Species: 4060 (Rauvolfia serpentina) [Search protein sequence]
MPRVKLGTQGLEVSKLGFGCMGLSPEEQGIAVIKEAFNCGITFFDTSDIY
GENGSNEELLGKALKQLPREKIQVGTKFGIHEIGFSGVKAKGTPDYVRSC
CEASLKRLDVDYIDLFYIHRIDTTVPIEITMGELKKLVEEGKIKYVGLSE
ASPDTIRRAHAVHPVTALQIEYSLWTRDIEDEIVPLCRQLGIGIVPYSPI
GRGLFWGKAIKEYYRIEALSQKHGCTPVQLALAWVLHQGEDVVPIPGTTK
IKNLHNNVGALKVKLTKEDLKEISDAVPWKFANTPPL
3D structure
PDB3v0t Crystal structure of perakine reductase, founding member of a novel aldo-keto reductase (AKR) subfamily that undergoes unique conformational changes during NADPH binding.
ChainA
Resolution2.333 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) D52 Y57 G94 H126
Catalytic site (residue number reindexed from 1) D45 Y50 G87 H119
Enzyme Commision number 1.1.1.317: perakine reductase.
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 ATR A S205 P206 I207 G208 L211 P278 G279 T280 T281 K282 N285 N288 N289 S198 P199 I200 G201 L204 P246 G247 T248 T249 K250 N253 N256 N257
Gene Ontology
Molecular Function
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0009820 alkaloid metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3v0t, PDBe:3v0t, PDBj:3v0t
PDBsum3v0t
PubMed22334702
UniProtQ3L181|PERR_RAUSE Perakine reductase (Gene Name=PR)

[Back to BioLiP]