[English] 日本語
![](img/lk-miru.gif)
- PDB-2wh8: Interaction of Mycobacterium tuberculosis CYP130 with heterocycli... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2wh8 | ||||||
---|---|---|---|---|---|---|---|
Title | Interaction of Mycobacterium tuberculosis CYP130 with heterocyclic arylamines | ||||||
![]() | PUTATIVE CYTOCHROME P450 130 | ||||||
![]() | OXIDOREDUCTASE / IRON / HEME / MONOOXYGENASE / METAL-BINDING / HYPOTHETICAL PROTEIN | ||||||
Function / homology | ![]() Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen / cell wall / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / cholest-4-en-3-one 26-monooxygenase activity / steroid hydroxylase activity / cholesterol catabolic process / monooxygenase activity / peptidoglycan-based cell wall / iron ion binding / heme binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Podust, L.M. / Ouellet, H. / von Kries, J.P. / Ortiz de Montellano, P.R. | ||||||
![]() | ![]() Title: Interaction of Mycobacterium tuberculosis CYP130 with heterocyclic arylamines. Authors: Podust, L.M. / Ouellet, H. / von Kries, J.P. / de Montellano, P.R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 331.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 267.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.9 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 2.9 MB | Display | |
Data in XML | ![]() | 70.7 KB | Display | |
Data in CIF | ![]() | 97.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2wgyC ![]() 2whfC ![]() 2uuqS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 45705.566 Da / Num. of mol.: 4 / Fragment: RESIDUES 2-405 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q11062, UniProt: P9WPN5*PLUS, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen #2: Chemical | ChemComp-HEM / #3: Chemical | ChemComp-II2 / #4: Water | ChemComp-HOH / | Sequence details | 6 HIS-TAG RESIDUES ARE ADDED AT THE N-TERMINUS. A 406 SER AND A 407 ARG ARE INTRODUCED AT THE C- ...6 HIS-TAG RESIDUES ARE ADDED AT THE N-TERMINUS. A 406 SER AND A 407 ARG ARE INTRODUCED | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41 % / Description: NONE |
---|---|
Crystal grow | pH: 5 Details: 14% PEG 4000, 0.1M NA ACETATE, PH 5.0, 200 MM AMMONIUM SULFATE, 1% ISOPROPYL ALCOHOL |
-Data collection
Diffraction | Mean temperature: 110 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Dec 6, 2008 / Details: MIRRORS |
Radiation | Monochromator: SI (111) DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.11587 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 164200 / % possible obs: 96 % / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Biso Wilson estimate: 21.2 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 19.9 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 2.1 / % possible all: 93.1 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2UUQ Resolution: 1.7→89.44 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.939 / SU B: 5.886 / SU ML: 0.089 / Cross valid method: THROUGHOUT / ESU R: 0.267 / ESU R Free: 0.141 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DISORDERED REGIONS WERE OMITTED FROM THE STRUCTURE
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 22.151 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→89.44 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|