2Q95

E. coli methionine aminopeptidase Mn-form with inhibitor A05


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.214 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop flexibility in selective inhibition of bacterial enzymes.

Ma, Z.Q.Xie, S.X.Huang, Q.Q.Nan, F.J.Hurley, T.D.Ye, Q.Z.

(2007) BMC Struct Biol 7: 84-84

  • DOI: https://doi.org/10.1186/1472-6807-7-84
  • Primary Citation of Related Structures:  
    2Q92, 2Q93, 2Q94, 2Q95, 2Q96

  • PubMed Abstract: 

    Methionine aminopeptidase is a potential target of future antibacterial and anticancer drugs. Structural analysis of complexes of the enzyme with its inhibitors provides valuable information for structure-based drug design efforts.


  • Organizational Affiliation

    High Throughput Screening Laboratory, University of Kansas, Lawrence, Kansas 66047, USA. zeqiang.ma@vanderbilt.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Methionine aminopeptidase263Escherichia coliMutation(s): 0 
Gene Names: map
EC: 3.4.11.18
UniProt
Find proteins for P0AE18 (Escherichia coli (strain K12))
Explore P0AE18 
Go to UniProtKB:  P0AE18
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AE18
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
A05 Binding MOAD:  2Q95 IC50: 1600 (nM) from 1 assay(s)
BindingDB:  2Q95 IC50: min: 1560, max: 4.86e+4 (nM) from 4 assay(s)
PDBBind:  2Q95 IC50: 1600 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.214 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.847α = 90
b = 62.373β = 108.39
c = 52.422γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
MOLREPphasing
CNSrefinement
PDB_EXTRACTdata extraction
MOSFLMdata reduction

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

  • Released Date: 2008-01-01 
  • Deposition Author(s): Ye, Q.-Z.

Revision History  (Full details and data files)

  • Version 1.0: 2008-01-01
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description