+Open data
-Basic information
Entry | Database: PDB / ID: 1f6g | ||||||
---|---|---|---|---|---|---|---|
Title | POTASSIUM CHANNEL (KCSA) FULL-LENGTH FOLD | ||||||
Components | VOLTAGE-GATED POTASSIUM CHANNEL | ||||||
Keywords | PROTON TRANSPORT / MEMBRANE PROTEIN / POTASSIUM CHANNEL / INTEGRAL MEMBRANE PROTEIN / CYTOPLASMIC DOMAINS | ||||||
Function / homology | Potassium channel domain / Ion channel / monoatomic ion transmembrane transport / identical protein binding / plasma membrane / pH-gated potassium channel KcsA Function and homology information | ||||||
Biological species | Streptomyces lividans (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Cortes, D.M. / Perozo, E. | ||||||
Citation | Journal: J.Gen.Physiol. / Year: 2001 Title: Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. Authors: Cortes, D.M. / Cuello, L.G. / Perozo, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1f6g.cif.gz | 112 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1f6g.ent.gz | 103.8 KB | Display | PDB format |
PDBx/mmJSON format | 1f6g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f6/1f6g ftp://data.pdbj.org/pub/pdb/validation_reports/f6/1f6g | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 17535.375 Da / Num. of mol.: 4 / Fragment: FULL-LENGTH CHANNEL / Mutation: CYS SCANNING: 5-24, 120-160 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces lividans (bacteria) / Plasmid: PQE32 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A334 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: This structure was determined using secondary structure assignments from frequency analysis of solvent accessibility data and tertiary and quaternary structural information from spin-spin dipolar couplings |
-Sample preparation
Details | Contents: 50-100 uM KcsA, PBS pH 7.2, reconstituted into asolectin vesicles at a 1:500 protein:lipid ratio (molar) Solvent system: 100% H2O |
---|---|
Sample conditions | Ionic strength: 50-100 mM / pH: 7.2 / Pressure: ambient / Temperature: 293 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker EMX / Manufacturer: Bruker / Model: EMX / Field strength: 3400 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: structures are based on a total of 438 restraints, with 84 intra-subunit distance constraints per subunit and 15 inter-subunit constraints | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 32 / Conformers submitted total number: 8 |