1ALW

INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.210 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding.

Lin, G.D.Chattopadhyay, D.Maki, M.Wang, K.K.Carson, M.Jin, L.Yuen, P.W.Takano, E.Hatanaka, M.DeLucas, L.J.Narayana, S.V.

(1997) Nat Struct Biol 4: 539-547

  • DOI: https://doi.org/10.1038/nsb0797-539
  • Primary Citation of Related Structures:  
    1ALV, 1ALW

  • PubMed Abstract: 

    The three dimensional structure of calcium-bound domain VI of porcine calpain has been determined to 1.9 A resolution. The crystal structure reveals five EF-hands, one more than previously suggested. There are two EF-hand pairs, one pair (EF1-EF2) displays an 'open' conformation and the other (EF3-EF4) a 'closed' conformation. Unusually, a calcium atom is found at the C-terminal end of the calcium binding loop of EF4. With two additional residues in the calcium binding loop, the fifth EF-hand (EF5) is in a 'closed' conformation. EF5 pairs up with the corresponding fifth EF-hand of a non-crystallographically related molecule. Considering the EF5's role in a homodimer formation of domain VI, we suggest a model for the assembly of heterodimeric calpain. The crystal structure of a Ca2+ bound domain VI-inhibitor (PD150606) complex has been refined to 2.1 A resolution. A possible mode for calpain inhibition is discussed.


  • Organizational Affiliation

    Center for Macromolecular Crystallography, University of Alabama at Birmingham 35294, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CALPAIN
A, B
173Sus scrofaMutation(s): 0 
UniProt
Find proteins for P04574 (Sus scrofa)
Explore P04574 
Go to UniProtKB:  P04574
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04574
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ISA
Query on ISA

Download Ideal Coordinates CCD File 
G [auth A],
L [auth B]
3-(4-IODO-PHENYL)-2-MERCAPTO-PROPIONIC ACID
C9 H9 I O2 S
MXQYDIIKDPMYMF-QMMMGPOBSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
C [auth A]
D [auth A]
E [auth A]
F [auth A]
H [auth B]
C [auth A],
D [auth A],
E [auth A],
F [auth A],
H [auth B],
I [auth B],
J [auth B],
K [auth B]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
ISA PDBBind:  1ALW Ki: 300 (nM) from 1 assay(s)
Binding MOAD:  1ALW Ki: 300 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.210 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.87α = 90
b = 80.46β = 91.2
c = 57.08γ = 90
Software Package:
Software NamePurpose
PHASESphasing
X-PLORrefinement
X-GENdata reduction
X-GENdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-06-10
    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: 2012-05-02
    Changes: Structure summary
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references, Derived calculations, Refinement description