2AAT

2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Observed: 0.220 

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This is version 1.5 of the entry. See complete history. 


Literature

2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.

Smith, D.L., Almo, S.C., Toney, M.D., Ringe, D.

(1989) Biochemistry 28: 8161-8167

  • DOI: https://doi.org/10.1021/bi00446a030
  • Primary Citation of Related Structures:  
    2AAT

  • PubMed Abstract: 

    The three-dimensional structure of a mutant of the aspartate aminotransferase from Escherichia coli, in which the active-site lysine has been substituted by alanine (K258A), has been determined at 2.8-A resolution by X-ray diffraction. The mutant enzyme contains pyridoxamine phosphate as cofactor. The structure is compared to that of the mitochondrial aspartate aminotransferase. The most striking differences, aside from the absence of the lysine side chain, occur in the positions of the pyridoxamine group and of tryptophan 140.

    • Organizational Affiliation: 

    Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ASPARTATE AMINOTRANSFERASE396Escherichia coliMutation(s): 1 
EC: 2.6.1.1
UniProt
Find proteins for P00509 (Escherichia coli (strain K12))
Explore P00509 
Go to UniProtKB:  P00509
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00509
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PMP
Query on PMP
Download Ideal Coordinates CCD File 
C [auth A]4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
C8 H13 N2 O5 P
ZMJGSOSNSPKHNH-UHFFFAOYSA-N
SO4
Query on SO4
Download Ideal Coordinates CCD File 
B [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Observed: 0.220 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 156.8α = 90
b = 86.74β = 90
c = 79.84γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1989-10-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2012-07-25
    Changes: Structure summary
  • Version 1.4: 2020-07-29
    Changes: Database references, Derived calculations, Other, Structure summary
  • Version 1.5: 2024-02-14
    Changes: Data collection, Database references