[English] 日本語
![](img/lk-miru.gif)
- PDB-1uh5: Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2ang... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1uh5 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2angstroms | ||||||
![]() | enoyl-ACP reductase | ||||||
![]() | OXIDOREDUCTASE / FabI / Triclosan / P.falciparum / Enoyl-ACP reductase / NAD+ | ||||||
Function / homology | ![]() enoyl-[acyl-carrier-protein] reductase (NADH) activity / fatty acid biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Swarnamukhi, P.L. / Kapoor, M. / Surolia, N. / Surolia, A. / Suguna, K. | ||||||
![]() | ![]() Title: Structural basis for the variation in triclosan affinity to enoyl reductases. Authors: Pidugu, L.S. / Kapoor, M. / Surolia, N. / Surolia, A. / Suguna, K. #1: Journal: Biochem.J. / Year: 2004 Title: Kinetic and structural analysis of the increased affinity of enoyl-ACP (acyl-carrier protein) reductase for triclosan in the presence of NAD+ Authors: Kapoor, M. / Swarnamukhi, P.L. / Surolia, N. / Suguna, K. / Surolia, A. | ||||||
History |
| ||||||
Remark 750 | TURN Determination method: author determined |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 130.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 99.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 25.5 KB | Display | |
Data in CIF | ![]() | 34.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1v35C ![]() 1enoS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | The functional tetramer is generated by the two fold axis: -y+a, -x+b, -z+c/2 |
-
Components
#1: Protein | Mass: 37244.184 Da / Num. of mol.: 2 / Fragment: residues 96-424 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: FabI / Plasmid: pET28a(+) / Species (production host): Escherichia coli / Production host: ![]() ![]() References: UniProt: Q6LFB9, UniProt: Q9BJJ9*PLUS, enoyl-[acyl-carrier-protein] reductase (NADH) #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 56.8 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: sodium acetate, Ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 21, 2002 / Details: osmic mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 37772 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 7.2 % / Biso Wilson estimate: 26 Å2 / Rmerge(I) obs: 0.101 / Rsym value: 0.109 / Net I/σ(I): 20.2 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 7 % / Rmerge(I) obs: 0.358 / Mean I/σ(I) obs: 7.8 / Rsym value: 0.388 / % possible all: 99.3 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ENO Resolution: 2.2→17.21 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 543563.28 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 84.3064 Å2 / ksol: 0.390794 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.9 Å2
| ||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→17.21 Å
| ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.012 / Total num. of bins used: 6
| ||||||||||||||||||||||||||||||||||||
Xplor file |
|