+Open data
-Basic information
Entry | Database: PDB / ID: 2gqm | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of Human Cu(I)-Sco1 | ||||||
Components | SCO1 protein homolog, mitochondrial | ||||||
Keywords | METAL TRANSPORT / Thioredoxin-like fold / metalloprotein / Structural Genomics / Structural Proteomics in Europe / SPINE | ||||||
Function / homology | Function and homology information copper chaperone activity / mitochondrial cytochrome c oxidase assembly / Respiratory electron transport / myofibril / intracellular copper ion homeostasis / TP53 Regulates Metabolic Genes / Cytoprotection by HMOX1 / mitochondrial inner membrane / copper ion binding / mitochondrion Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Banci, L. / Bertini, I. / Calderone, V. / Ciofi-Baffoni, S. / Mangani, S. / Palumaa, P. / Martinelli, M. / Wang, S. / Structural Proteomics in Europe (SPINE) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2006 Title: A hint for the function of human Sco1 from different structures. Authors: Banci, L. / Bertini, I. / Calderone, V. / Ciofi-Baffoni, S. / Mangani, S. / Martinelli, M. / Palumaa, P. / Wang, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2gqm.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2gqm.ent.gz | 1.5 MB | Display | PDB format |
PDBx/mmJSON format | 2gqm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gq/2gqm ftp://data.pdbj.org/pub/pdb/validation_reports/gq/2gqm | HTTPS FTP |
---|
-Related structure data
Related structure data | 2ggtC 2gqkC 2gqlC 2gt5C 2gt6C 2gvpC C: citing same article (ref.) |
---|---|
Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 19712.277 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN (residues 132-301) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SCO1, SCOD1 / Plasmid: pET6-30A / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21DE3 GOLD / References: UniProt: O75880 |
---|---|
#2: Chemical | ChemComp-CU1 / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: 50mM sodium phosphate / pH: 7.2 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics / Software ordinal: 1 | |||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 350 / Conformers submitted total number: 30 |