Structure of PDB 1e3j Chain A

Receptor sequence
>1e3jA (length=348) Species: 77855 (Bemisia argentifolii) [Search protein sequence]
DNLSAVLYKQNDLRLEQRPIPEPKEDEVLLQMAYVGICGSDVHYYEHGRI
ADFIVKDPMVIGHEASGTVVKVGKNVKHLKKGDRVAVEPGVPCRRCQFCK
EGKYNLCPDLTFCATPPDDGNLARYYVHAADFCHKLPDNVSLEEGALLEP
LSVGVHACRRAGVQLGTTVLVIGAGPIGLVSVLAAKAYGAFVVCTARSPR
RLEVAKNCGADVTLVVDPAKEEESSIIERIRSAIGDLPNVTIDCSGNEKC
ITIGINITRTGGTLMLVGMGSQMVTVPLVNACAREIDIKSVFRYCNDYPI
ALEMVASGRCNVKQLVTHSFKLEQTVDAFEAARKKADNTIKVMISCRQ
3D structure
PDB1e3j Crystal Structure of Nadp(H)-Dependent Ketose Reductase from Besimia Argentifolii at 2.3 Angstrom Resolution
ChainA
Resolution2.3 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) C41 G42 S43 H46 H66 E67 C96 C99 C102 C110 T114 P153 G157 K344
Catalytic site (residue number reindexed from 1) C38 G39 S40 H43 H63 E64 C93 C96 C99 C107 T111 P150 G154 K341
Enzyme Commision number ?
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 ZN A C96 C99 C102 C110 C93 C96 C99 C107
BS02 ZN A C41 H66 E67 C38 H63 E64
BS03 PO4 A A177 A199 R200 S201 R204 A174 A196 R197 S198 R201
Gene Ontology
Molecular Function
GO:0003939 L-iditol 2-dehydrogenase (NAD+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
Biological Process
GO:0006062 sorbitol catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1e3j, PDBe:1e3j, PDBj:1e3j
PDBsum1e3j
PubMed11237597
UniProtO96496

[Back to BioLiP]