3MX7

Crystal Structure Analysis of Human FAIM-NTD


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.178 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The structure of human Fas apoptotic inhibitory molecule

Li, G.Qu, L.Meng, G.Bai, X.Dai, K.Zheng, X.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fas apoptotic inhibitory molecule 190Homo sapiensMutation(s): 0 
Gene Names: FAIMFAIM1
UniProt & NIH Common Fund Data Resources
Find proteins for Q9NVQ4 (Homo sapiens)
Explore Q9NVQ4 
Go to UniProtKB:  Q9NVQ4
PHAROS:  Q9NVQ4
GTEx:  ENSG00000158234 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9NVQ4
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.178 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 57.17α = 90
b = 57.17β = 90
c = 69.946γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
SOLVEphasing
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-05-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references