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2V0I

Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 17-ID
Synchrotron siteAPS
Beamline17-ID
Temperature [K]100
Detector technologyCCD
Collection date2003-11-01
DetectorADSC CCD
Spacegroup nameP 63 2 2
Unit cell lengths107.808, 107.808, 233.876
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution119.520 - 1.890
R-factor0.194
Rwork0.193
R-free0.21000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2v0h
RMSD bond length0.008
RMSD bond angle1.266
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.970
High resolution limit [Å]1.9001.900
Rmerge0.0700.320
Number of reflections64262
<I/σ(I)>37.94.5
Completeness [%]99.199.9
Redundancy9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
161.2-1.8M AMMONIUM SULFATE, 2%PEG-400, 0.1M MES PH 5.2-6.1, 20 MM MGCL2, 10 MM UDP-GLCNAC

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