[English] 日本語
![](img/lk-miru.gif)
- PDB-2w0a: CYP51 of M. tuberculosis bound to an inhibitor N-[(1S)-2-METHYL-1... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2w0a | ||||||
---|---|---|---|---|---|---|---|
Title | CYP51 of M. tuberculosis bound to an inhibitor N-[(1S)-2-METHYL-1-(PYRIDIN-4-YLCARBAMOYL)PROPYL]CYCLOHEXANECARBOXAMIDE | ||||||
![]() | CYTOCHROME P450 51 | ||||||
![]() | OXIDOREDUCTASE / STEROID BIOSYNTHESIS / PROTEIN-INHIBITOR COMPLEX / METAL-BINDING / LIPID SYNTHESIS / NADP / IRON / HEME / CYTOPLASM / MONOOXYGENASE / STEROL BIOSYNTHESIS | ||||||
Function / homology | ![]() sterol 14alpha-demethylase (ferredoxin) / sterol 14alpha-demethylase / sterol 14-demethylase activity / sterol biosynthetic process / sterol metabolic process / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / monooxygenase activity / oxidoreductase activity / iron ion binding / heme binding ...sterol 14alpha-demethylase (ferredoxin) / sterol 14alpha-demethylase / sterol 14-demethylase activity / sterol biosynthetic process / sterol metabolic process / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / monooxygenase activity / oxidoreductase activity / iron ion binding / heme binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Podust, L.M. | ||||||
![]() | ![]() Title: Trypanosoma Cruzi Cyp51 Inhibitor Derived from a Mycobacterium Tuberculosis Screen Hit. Authors: Chen, C.-K. / Doyle, P.S. / Yermalitskaya, L.V. / Mackey, Z.B. / Ang, K.K.H. / Mckerrow, J.H. / Podust, L.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 194.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 152.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 2w09C ![]() 2w0bC ![]() 1x8vS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 51491.312 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: 4XHIS TAG AT THE C-TERMINUS / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A512, UniProt: P9WPP9*PLUS, sterol 14alpha-demethylase | ||||
---|---|---|---|---|---|
#2: Chemical | ChemComp-HEM / | ||||
#3: Chemical | ChemComp-CII / | ||||
#4: Water | ChemComp-HOH / | ||||
Compound details | ENGINEEREDNonpolymer details | NONE (C11): COORDINATION BOND TO THE HEME IRON PROTOPORPHYRIN IX CONTAINING FE (HEM): THIOLATE BOND ...NONE (C11): COORDINATI | Sequence details | MUTATIONS C37L, C442A ENGINEERED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 40 % / Description: NONE |
---|---|
Crystal grow | Temperature: 296 K / pH: 7.5 Details: 15% PEG 4000, 2% ISOPROPANOL, 0.1 M HEPES, PH=7.5, T=23 C |
-Data collection
Diffraction | Mean temperature: 110 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 5, 2006 Details: SAGITTAL FOCUSING CRYSTAL AND VERTICALLY FOCUSING DOUBLE MIRROR |
Radiation | Monochromator: SI (220) DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→50 Å / Num. obs: 53704 / % possible obs: 93.8 % / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Biso Wilson estimate: 18.7 Å2 / Rmerge(I) obs: 0.01 / Net I/σ(I): 32.5 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 3.4 / % possible all: 77.7 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1X8V Resolution: 1.6→67.73 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.937 / SU B: 3.69 / SU ML: 0.06 / Cross valid method: THROUGHOUT / ESU R: 0.162 / ESU R Free: 0.11 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-2, 90-105, 217-221, 235-236 ARE DISORDERED 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: 20.36 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→67.73 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|