1LBU

HYDROLASE METALLO (ZN) DD-PEPTIDASE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.164 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Streptomyces Albus G D-Ala-A-Ala Carboxypeptidase

Charlier, P., Wery, J.-P., Dideberg, O., Frere, J.-M.

(2004) Handbook Of Metalloproteins 3: 164


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MURAMOYL-PENTAPEPTIDE CARBOXYPEPTIDASE213Streptomyces albus GMutation(s): 0 
EC: 3.4.17.8
UniProt
Find proteins for P00733 (Streptomyces albus G)
Explore P00733 
Go to UniProtKB:  P00733
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00733
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN
Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.164 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 51.08α = 90
b = 49.7β = 100.6
c = 38.65γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-11-08
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance