[English] 日本語
![](img/lk-miru.gif)
- PDB-4cgl: Leishmania major N-myristoyltransferase in complex with an aminoa... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 4cgl | ||||||
---|---|---|---|---|---|---|---|
Title | Leishmania major N-myristoyltransferase in complex with an aminoacylpyrrolidine inhibitor | ||||||
![]() | GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE | ||||||
![]() | TRANSFERASE / MYRISTOYLATION / INHIBITOR / AMINOACYLPYRROLIDINE | ||||||
Function / homology | ![]() glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Brannigan, J.A. / Roberts, S.M. / Bell, A.S. / Hutton, J.A. / Smith, D.F. / Tate, E.W. / Leatherbarrow, R.J. / Wilkinson, A.J. | ||||||
![]() | ![]() Title: Diverse Modes of Binding in Structures of Leishmania Major N-Myristoyltransferase with Selective Inhibitors Authors: Brannigan, J.A. / Roberts, S.M. / Bell, A.S. / Hutton, J.A. / Hodgkinson, M.R. / Tate, E.W. / Leatherbarrow, R.J. / Smith, D.F. / Wilkinson, A.J. #1: ![]() Title: Structure-Based Design of Potent and Selective Leishmania N- Myristoyltransferase Inhibitors. Authors: Hutton, J.A. / Goncalves, V. / Brannigan, J.A. / Paape, D. / Wright, M.H. / Waugh, T.M. / Roberts, S.M. / Bell, A.S. / Wilkinson, A.J. / Smith, D.F. / Leatherbarrow, R.J. / Tate, E.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 112.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 85.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 982.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 990.2 KB | Display | |
Data in XML | ![]() | 22.3 KB | Display | |
Data in CIF | ![]() | 33.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 47510.129 Da / Num. of mol.: 1 / Fragment: RESIDUES 11-421 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q4Q5S8, glycylpeptide N-tetradecanoyltransferase |
---|---|
#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-A6K / ( |
#4: Chemical | ChemComp-MYA / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 45 % / Description: NONE |
---|---|
Crystal grow | pH: 5.5 Details: 30% PEG 1500, 0.2 M NACL, 0.1 M NA CACODYLATE, PH 5.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 8, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9173 Å / Relative weight: 1 |
Reflection | Resolution: 1.48→46 Å / Num. obs: 68755 / % possible obs: 96 % / Observed criterion σ(I): 1.6 / Redundancy: 4.2 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 1.48→1.51 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.96 / Mean I/σ(I) obs: 1.6 / % possible all: 96 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 1.48→49.15 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.945 / SU B: 2.265 / SU ML: 0.081 / Cross valid method: THROUGHOUT / ESU R: 0.086 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.774 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.48→49.15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|