[English] 日本語
![](img/lk-miru.gif)
- PDB-1q7c: The structure of betaketoacyl-[ACP] reductase Y151F mutant in com... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1q7c | ||||||
---|---|---|---|---|---|---|---|
Title | The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment | ||||||
![]() | 3-oxoacyl-[acyl-carrier protein] reductase | ||||||
![]() | OXIDOREDUCTASE / oxoacyl reductase / NADP+ / crystal structure | ||||||
Function / homology | ![]() biotin biosynthetic process / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / fatty acid elongation / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / lipid biosynthetic process / fatty acid biosynthetic process / NAD binding / NADP binding / identical protein binding ...biotin biosynthetic process / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / fatty acid elongation / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / lipid biosynthetic process / fatty acid biosynthetic process / NAD binding / NADP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Price, A.C. / Zhang, Y.-M. / Rock, C.O. / White, S.M. | ||||||
![]() | ![]() Title: Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in FabG Authors: Price, A.C. / Zhang, Y.-M. / Rock, C.O. / White, S.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 101 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 78.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 20.4 KB | Display | |
Data in CIF | ![]() | 27.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||||
Unit cell |
| ||||||||||
Details | The biological assembly is the tetramer formed from the dimer in the ASU by the two fold axis: -x, y, -z+1/2 |
-
Components
#1: Protein | Mass: 25571.277 Da / Num. of mol.: 2 / Mutation: Y141F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P25716, UniProt: P0AEK2*PLUS, 3-oxoacyl-[acyl-carrier-protein] reductase #2: Chemical | #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.6 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Method: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.6 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: ENRAF-NONIUS / Detector: CCD / Date: Feb 5, 2003 / Details: Osmic mirrors |
Radiation | Monochromator: Osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→65.8 Å / Num. all: 17095 / Num. obs: 17095 / % possible obs: 99.95 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2.5→2.61 Å / % possible all: 100 |
Reflection | *PLUS Highest resolution: 2.5 Å / Redundancy: 10.1 % / Num. measured all: 172466 / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS % possible obs: 100 % / Redundancy: 7.9 % / Num. unique obs: 2163 / Rmerge(I) obs: 0.174 / Mean I/σ(I) obs: 3.4 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||||||||||||
Displacement parameters |
| ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→65.8 Å
| ||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.252 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|