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2GZ5

Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.2.2
Synchrotron siteALS
Beamline8.2.2
Temperature [K]100
Detector technologyCCD
Collection date2004-07-04
DetectorADSC QUANTUM 315
Wavelength(s)0.977
Spacegroup nameP 1 21 1
Unit cell lengths47.568, 77.689, 48.644
Unit cell angles90.00, 90.63, 90.00
Refinement procedure
Resolution20.000 - 1.100
R-factor0.135
Rwork0.117
R-free0.14500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2b3k
RMSD bond length0.031
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareGLRF
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.120
High resolution limit [Å]1.1001.100
Rmerge0.0500.311
Number of reflections244734
<I/σ(I)>2.7
Completeness [%]95.565.2
Redundancy43.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP2984-6% PEG 10,000, 100 mM HEPES, pH 6.0 in equal volume of the protein 10 mg/ml in 25 mM HEPES, pH 8.0, 5 mM methionine and 150 mM KCl. To the apo crystals, 1mM cobalt chloride and 2 mM ovalicin were added, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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