2C1Q

X-ray structure of biotin binding protein from chicken

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history. 


Literature

Structure and Characterization of a Novel Chicken Biotin-Binding Protein a (Bbp-A).

Hytonen, V.P., Maatta, J.A.E., Niskanen, E.A., Huuskonen, J., Helttunen, K.J., Halling, K.K., Nordlund, H.R., Rissanen, K., Johnson, M.S., Salminen, T.A., Kulomaa, M.S., Laitinen, O.H., Airenne, T.T.

(2007) BMC Struct Biol 7: 8

  • DOI: https://doi.org/10.1186/1472-6807-7-8
  • Primary Citation of Related Structures:  
    2C1Q, 2C1S

  • PubMed Abstract: 

    The chicken genome contains a BBP-A gene showing similar characteristics to avidin family genes. In a previous study we reported that the BBP-A gene may encode a biotin-binding protein due to the high sequence similarity with chicken avidin, especially at regions encoding residues known to be located at the ligand-binding site of avidin.

    • Organizational Affiliation: 

    NanoScience Center, Department of Biological and Environmental Science, P.O. Box 35 (YAB), FI-40014 University of Jyväskylä, Finland. veshyto@mat.ethz.ch


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BIOTIN BINDING PROTEIN A126Gallus gallusMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
BTN Binding MOAD:  2C1Q Kd: 1.00e-4 (nM) from 1 assay(s)
PDBBind:  2C1Q Kd: 1.00e-4 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 
  • Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 61.653α = 90
b = 61.653β = 90
c = 179.659γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
AMoREphasing

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: 2007-02-20
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-17
    Changes: Data collection
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description