3EDH

Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.25 Å
  • R-Value Free: 0.172 
  • R-Value Work: 0.140 
  • R-Value Observed: 0.142 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases

Mac Sweeney, A.Parrado, S.G.Vinzenz, D.Bernardi, A.Hein, A.Bodendorf, U.Erbel, P.Logel, C.Gerhartz, B.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bone morphogenetic protein 1201Homo sapiensMutation(s): 0 
Gene Names: BMP1PCOLC
EC: 3.4.24.19
UniProt & NIH Common Fund Data Resources
Find proteins for P13497 (Homo sapiens)
Explore P13497 
Go to UniProtKB:  P13497
PHAROS:  P13497
GTEx:  ENSG00000168487 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP13497
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.25 Å
  • R-Value Free: 0.172 
  • R-Value Work: 0.140 
  • R-Value Observed: 0.142 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.499α = 90
b = 59.093β = 90
c = 69.451γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-09-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description