2RC5

Refined structure of FNR from Leptospira interrogans

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.43 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.225 

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This is version 1.2 of the entry. See complete history. 


Literature

Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+.

Nascimento, A.S., Catalano-Dupuy, D.L., Bernardes, A., Neto, M.O., Santos, M.A., Ceccarelli, E.A., Polikarpov, I.

(2007) BMC Struct Biol 7: 69-69

  • DOI: https://doi.org/10.1186/1472-6807-7-69
  • Primary Citation of Related Structures:  
    2RC5, 2RC6

  • PubMed Abstract: 

    Ferredoxin-NADP(H) reductases (FNRs) are flavoenzymes that catalyze the electron transfer between NADP(H) and the proteins ferredoxin or flavodoxin. A number of structural features distinguish plant and bacterial FNRs, one of which is the mode of the cofactor FAD binding. Leptospira interrogans is a spirochaete parasitic bacterium capable of infecting humans and mammals in general. Leptospira interrogans FNR (LepFNR) displays low sequence identity with plant (34% with Zea mays) and bacterial (31% with Escherichia coli) FNRs. However, LepFNR contains all consensus sequences that define the plastidic class FNRs.

    • Organizational Affiliation: 

    Instituto de Física de São Carlos, Universidade de São Paulo, Av, Trabalhador Saocarlense 400, São Carlos, SP, 13560-970, Brazil. asnascimento@if.sc.usp.br


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ferredoxin-NADP reductase
A, B, C, D
314Leptospira interrogansMutation(s): 0 
EC: 1.18.1.2
UniProt
Find proteins for Q8EY89 (Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601))
Explore Q8EY89 
Go to UniProtKB:  Q8EY89
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8EY89
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
FAD
Query on FAD
Download Ideal Coordinates CCD File 
H [auth A],
J [auth B],
N [auth C],
P [auth D]		FLAVIN-ADENINE DINUCLEOTIDE
C27 H33 N9 O15 P2
VWWQXMAJTJZDQX-UYBVJOGSSA-N
SO4
Query on SO4
Download Ideal Coordinates CCD File 
E [auth A]
F [auth A]
I [auth B]
K [auth C]
L [auth C]
E [auth A],
F [auth A],
I [auth B],
K [auth C],
L [auth C],
M [auth C],
O [auth D]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
ZN
Query on ZN
Download Ideal Coordinates CCD File 
G [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.43 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.225 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 65.112α = 90
b = 111.832β = 92.76
c = 89.913γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-03-25
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references, Derived calculations