1ERZ

CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.201 
  • R-Value Work: 0.176 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases.

Nakai, T.Hasegawa, T.Yamashita, E.Yamamoto, M.Kumasaka, T.Ueki, T.Nanba, H.Ikenaka, Y.Takahashi, S.Sato, M.Tsukihara, T.

(2000) Structure 8: 729-737

  • DOI: https://doi.org/10.1016/s0969-2126(00)00160-x
  • Primary Citation of Related Structures:  
    1ERZ

  • PubMed Abstract: 

    N-carbamyl-D-amino acid amidohydrolase (DCase) catalyzes the hydrolysis of N-carbamyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics. To understand the catalytic mechanism of N-carbamyl-D-amino acid hydrolysis, the substrate specificity and thermostability of the enzyme, we have determined the structure of DCase from Agrobacterium sp. strain KNK712.


  • Organizational Affiliation

    Kaneka Corporation, Takasago-cho, Takasago, 676-8688, Japan. tnakai@kaneka.co.jp


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE
A, B
303Agrobacterium sp. KNK712Mutation(s): 0 
EC: 3.5.1.77
UniProt
Find proteins for P60327 (Agrobacterium sp. (strain KNK712))
Explore P60327 
Go to UniProtKB:  P60327
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP60327
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.201 
  • R-Value Work: 0.176 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.84α = 90
b = 137.83β = 90
c = 68.39γ = 90
Software Package:
Software NamePurpose
MLPHAREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-04-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2021-02-03
    Changes: Database references
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references