[English] 日本語
Yorodumi- 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 | ||||||||||||
Components | (BT-CD domains of human acetyl-CoA carboxylase) x 2 | ||||||||||||
Keywords | LIGASE / Carboxylase / carrier protein-dependent enzyme / fatty acid metabolism / multienzyme | ||||||||||||
Function / homology | : Function and homology information | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.7 Å | ||||||||||||
Authors | Stuttfeld, E. / Hunkeler, M. / Hagmann, A. / Imseng, S. / Maier, T. | ||||||||||||
Funding support | Switzerland, 3items
| ||||||||||||
Citation | Journal: Nat Commun / Year: 2016 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: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5i87.cif.gz | 194.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5i87.ent.gz | 163.7 KB | Display | PDB format |
PDBx/mmJSON format | 5i87.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i8/5i87 ftp://data.pdbj.org/pub/pdb/validation_reports/i8/5i87 | 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.) Homo sapiens (human) / Cell line (production host): Sf21 / Production host: Spodoptera frugiperda (fall armyworm) / References: acetyl-CoA carboxylase |
---|---|
#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.) Homo sapiens (human) / Cell line (production host): Sf21 / Production host: Spodoptera frugiperda (fall armyworm) / References: acetyl-CoA carboxylase |
#3: Chemical | ChemComp-CD / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-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: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å |
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: SAD / Resolution: 3.7→84.518 Å / SU ML: 0.91 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 51.48
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 |
|