5KET

Structure of the aldo-keto reductase from Coptotermes gestroi


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.239 
  • R-Value Observed: 0.242 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.6 of the entry. See complete history


Literature

The Coptotermes gestroi aldo-keto reductase: a multipurpose enzyme for biorefinery applications.

Tramontina, R.Franco Cairo, J.P.Liberato, M.V.Mandelli, F.Sousa, A.Santos, S.Rabelo, S.C.Campos, B.Ienczak, J.Ruller, R.Damasio, A.R.Squina, F.M.

(2017) Biotechnol Biofuels 10: 4-4

  • DOI: https://doi.org/10.1186/s13068-016-0688-6
  • Primary Citation of Related Structures:  
    5KET

  • PubMed Abstract: 

    In nature, termites can be considered as a model biological system for biofuel research based on their remarkable efficiency for lignocellulosic biomass conversion. Redox enzymes are of interest in second-generation ethanol production because they promote synergic enzymatic activity with classical hydrolases for lignocellulose saccharification and inactivate fermentation inhibitory compounds produced after lignocellulose pretreatment steps.


  • Organizational Affiliation

    Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Rua Giuseppe Máximo Scolfaro, no 10000 Campinas, SP Brazil ; Programa de Pós Graduação em Biociências e Tecnologia de Produtos Bioativos (BTPB)-Instituto de Biologia-CP 6109, Universidade Estadual de Campinas-UNICAMP, 13083-970 Campinas, SP Brazil.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aldo-keto reductase 1
A, B
340Coptotermes gestroiMutation(s): 0 
UniProt
Find proteins for A0A140CVV2 (Coptotermes gestroi)
Explore A0A140CVV2 
Go to UniProtKB:  A0A140CVV2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A140CVV2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NAP
Query on NAP

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
C21 H28 N7 O17 P3
XJLXINKUBYWONI-NNYOXOHSSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.239 
  • R-Value Observed: 0.242 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 131.141α = 90
b = 131.141β = 90
c = 290.657γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
Aimlessdata scaling
PHASERphasing
PDB_EXTRACTdata extraction
XDSdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Sao Paulo Research Foundation (FAPESP)Brazil2014/04105-4
Sao Paulo Research Foundation (FAPESP)Brazil2014/50371-8
Sao Paulo Research Foundation (FAPESP)Brazil2014/20576-7
Sao Paulo Research Foundation (FAPESP)Brazil2013/06336-0

Revision History  (Full details and data files)

  • Version 1.0: 2017-01-18
    Type: Initial release
  • Version 1.1: 2017-11-22
    Changes: Database references, Refinement description
  • Version 1.2: 2018-01-17
    Changes: Author supporting evidence
  • Version 1.3: 2018-01-31
    Changes: Data collection
  • Version 1.4: 2019-04-17
    Changes: Author supporting evidence, Data collection
  • Version 1.5: 2020-01-01
    Changes: Author supporting evidence
  • Version 1.6: 2023-09-27
    Changes: Data collection, Database references, Refinement description