1CPB | pdb_00001cpb

STRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Structure of carboxypeptidase B at 2-8 A resolution.

Schmid, M.F., Herriott, J.R.

(1976) J Mol Biology 103: 175-190


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CARBOXYPEPTIDASE B82Bos taurusMutation(s): 0 
EC: 3.4.17.2
UniProt
Find proteins for P00732 (Bos taurus)
Explore P00732 
Go to UniProtKB:  P00732
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00732
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CARBOXYPEPTIDASE B217Bos taurusMutation(s): 0 
EC: 3.4.17.2
UniProt
Find proteins for P00732 (Bos taurus)
Explore P00732 
Go to UniProtKB:  P00732
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00732
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.94α = 90
b = 54.94β = 90
c = 104.6γ = 120

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1977-11-14
    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: 2024-02-07
    Changes: Data collection, Database references, Other