1FBL

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Work: 0.217 
  • R-Value Observed: 0.217 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.

Li, J.Brick, P.O'Hare, M.C.Skarzynski, T.Lloyd, L.F.Curry, V.A.Clark, I.M.Bigg, H.F.Hazleman, B.L.Cawston, T.E.Blow, D.M.

(1995) Structure 3: 541-549

  • DOI: https://doi.org/10.1016/s0969-2126(01)00188-5
  • Primary Citation of Related Structures:  
    1FBL

  • PubMed Abstract: 

    The collagenases are members of the family of zinc-dependent enzymes known as the matrix metalloproteinases (MMPs). They are the only proteinases that specifically cleave the collagen triple helix, and are important in a large number of physiological and pathological processes. Structures are known for the N-terminal catalytic' domain of collagenases MMP-1 and MMP-8 and of stromelysin (MMP-3). This catalytic domain alone, which comprises about 150 amino acids, has no activity against collagen. A second domain, of 200 amino acids, is homologous to haemopexin, a haem-binding glycoprotein.


  • Organizational Affiliation

    Blackert Laboratory, Imperial College, London, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FIBROBLAST (INTERSTITIAL) COLLAGENASE (MMP-1)370Sus scrofaMutation(s): 0 
EC: 3.4.24.7
UniProt
Find proteins for P21692 (Sus scrofa)
Explore P21692 
Go to UniProtKB:  P21692
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP21692
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
HTA BindingDB:  1FBL Ki: min: 1, max: 10 (nM) from 3 assay(s)
IC50: min: 1.9, max: 20 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Work: 0.217 
  • R-Value Observed: 0.217 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 161.14α = 90
b = 161.14β = 90
c = 52.22γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-01-29
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2012-02-22
    Changes: Database references