[English] 日本語
![](img/lk-miru.gif)
- PDB-5i87: Crystal structure of BT-CD domains of human acetyl-CoA carboxylase -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 5i87 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Crystal structure of BT-CD domains of human acetyl-CoA carboxylase | ||||||||||||
![]() | (BT-CD domains of human acetyl-CoA carboxylase) x 2 | ||||||||||||
![]() | LIGASE / Carboxylase / carrier protein-dependent enzyme / fatty acid metabolism / multienzyme | ||||||||||||
Function / homology | : ![]() | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Stuttfeld, E. / Hunkeler, M. / Hagmann, A. / Imseng, S. / Maier, T. | ||||||||||||
Funding support | ![]()
| ||||||||||||
![]() | ![]() Title: The dynamic organization of fungal acetyl-CoA carboxylase. Authors: Hunkeler, M. / Stuttfeld, E. / Hagmann, A. / Imseng, S. / Maier, T. | ||||||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 194.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 163.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 371.8 KB | Display | |
Data in XML | ![]() | 23.2 KB | Display | |
Data in CIF | ![]() | 36.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 61548.770 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: 1. Due to the low resolution of the diffraction data, authors could not identify the correct numbering/type of the residues. The residue numbering is arbitrary. The one-letter sequence for ...Details: 1. Due to the low resolution of the diffraction data, authors could not identify the correct numbering/type of the residues. The residue numbering is arbitrary. The one-letter sequence for the protein corresponds to Uniprot accession Q13085 residues 622-1584. 2. Residues 753-818 of Uniprot accession Q13085 were replaced by a GSG linker in the crystallized construct. Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 56357.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: 1. Due to the low resolution of the diffraction data, authors could not identify the correct numbering/type of the residues. The residue numbering is arbitrary. The one-letter sequence for ...Details: 1. Due to the low resolution of the diffraction data, authors could not identify the correct numbering/type of the residues. The residue numbering is arbitrary. The one-letter sequence for the protein corresponds to Uniprot accession Q13085 residues 622-1584. 2. Residues 753-818 of Uniprot accession Q13085 were replaced by a GSG linker in the crystallized construct. Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-CD / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal grow | Temperature: 292.15 K / Method: vapor diffusion, sitting drop / pH: 6 / Details: MES, tri-potassium citrate, PEG10000 |
---|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 9, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.7→84.518 Å / Num. obs: 77629 / % possible obs: 99.8 % / Redundancy: 13.7 % / CC1/2: 1 / Rmerge(I) obs: 0.075 / Net I/σ(I): 21.24 |
Reflection shell | Resolution: 3.7→3.8 Å / Redundancy: 13.7 % / Rmerge(I) obs: 4.01 / Mean I/σ(I) obs: 1.07 / % possible all: 99.1 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.7→84.518 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|