- PDB-2wns: Human Orotate phosphoribosyltransferase (OPRTase) domain of Uridi... -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 2wns
Title
Human Orotate phosphoribosyltransferase (OPRTase) domain of Uridine 5' -monophosphate synthase (UMPS) in complex with its substrate orotidine 5'-monophosphate (OMP)
Mass: 18.015 Da / Num. of mol.: 237 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer details
OROTIDINE-5'-MONOPHOSPHATE (OMP): THE OROTIDINE 5-MONOPHOSPHATE, OMP, WAS RENAMED INTO DRG SINCE ...OROTIDINE-5'-MONOPHOSPHATE (OMP): THE OROTIDINE 5-MONOPHOSPHATE, OMP, WAS RENAMED INTO DRG SINCE THERE WAS A PROBLEM WITH THE REFMAC5 OMP DEFAULT DICTIONARY
Sequence details
THE SEQUENCE CONTAINS ONLY THE OROTATE PHOSPHORIBOSYLTRANSFERASE DOMAIN OF UMPS AND IS FURTHER CUT ...THE SEQUENCE CONTAINS ONLY THE OROTATE PHOSPHORIBOSYLTRANSFERASE DOMAIN OF UMPS AND IS FURTHER CUT BY SIX AA IN THE N-TERMINUS AND IN ADDITION CONTAINS AN C-TERMINAL HEXAHISTIDINE TAG.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 1.95 Å3/Da / Density % sol: 36.52 % / Description: NONE
Resolution: 1.9→37.06 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.927 / SU B: 3.909 / SU ML: 0.114 / Cross valid method: THROUGHOUT / ESU R: 0.173 / ESU R Free: 0.155 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.22791
1418
5 %
RANDOM
Rwork
0.18003
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obs
0.18244
26940
100 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK