+Open data
-Basic information
Entry | Database: PDB / ID: 1s6c | ||||||
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Title | Crystal structure of the complex between KChIP1 and Kv4.2 N1-30 | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / EF-hand | ||||||
Function / homology | Function and homology information Phase 1 - inactivation of fast Na+ channels / cardiac muscle cell action potential / Kv4.2-KChIP2 channel complex / A-type (transient outward) potassium channel activity / Voltage gated Potassium channels / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / potassium channel complex / : / perinuclear endoplasmic reticulum / positive regulation of action potential ...Phase 1 - inactivation of fast Na+ channels / cardiac muscle cell action potential / Kv4.2-KChIP2 channel complex / A-type (transient outward) potassium channel activity / Voltage gated Potassium channels / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / potassium channel complex / : / perinuclear endoplasmic reticulum / positive regulation of action potential / membrane repolarization / voltage-gated monoatomic ion channel activity / regulation of potassium ion transmembrane transport / postsynaptic specialization membrane / anchoring junction / action potential / neuronal cell body membrane / voltage-gated potassium channel activity / potassium channel activity / plasma membrane raft / locomotor rhythm / GABA-ergic synapse / potassium channel regulator activity / neuronal action potential / potassium ion transmembrane transport / voltage-gated potassium channel complex / extrinsic component of cytoplasmic side of plasma membrane / sensory perception of pain / T-tubule / caveola / muscle contraction / potassium ion transport / protein homooligomerization / sarcolemma / cellular response to mechanical stimulus / cellular response to xenobiotic stimulus / monoatomic ion channel activity / cellular response to hypoxia / postsynaptic membrane / perikaryon / transmembrane transporter binding / dendritic spine / neuronal cell body / glutamatergic synapse / calcium ion binding / dendrite / protein-containing complex binding / membrane / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Zhou, W. / Qian, Y. / Kunjilwar, K. / Pfaffinger, P.J. / Choe, S. | ||||||
Citation | Journal: Neuron / Year: 2004 Title: Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels. Authors: Zhou, W. / Qian, Y. / Kunjilwar, K. / Pfaffinger, P.J. / Choe, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s6c.cif.gz | 57.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s6c.ent.gz | 39.7 KB | Display | PDB format |
PDBx/mmJSON format | 1s6c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1s6c_validation.pdf.gz | 445.6 KB | Display | wwPDB validaton report |
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Full document | 1s6c_full_validation.pdf.gz | 450.1 KB | Display | |
Data in XML | 1s6c_validation.xml.gz | 11.8 KB | Display | |
Data in CIF | 1s6c_validation.cif.gz | 16 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s6/1s6c ftp://data.pdbj.org/pub/pdb/validation_reports/s6/1s6c | HTTPS FTP |
-Related structure data
Related structure data | 1g8iS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 21760.275 Da / Num. of mol.: 1 / Fragment: Core domain (Residues 34-216) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: KChIP1 / Plasmid: pHIS8 (pET28_mod) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (ED3) / References: UniProt: Q8R426 | ||
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#2: Protein/peptide | Mass: 2967.552 Da / Num. of mol.: 1 / Fragment: N-terminus (Residues 1-30) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: KCND2 / Plasmid: pHIS8 (pET28_mod) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q63881 | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.81 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 1000, magnesium nitrate, sodium cacodylate, DTT, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.044 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Aug 3, 2002 |
Radiation | Monochromator: Double Crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.044 Å / Relative weight: 1 |
Reflection | Resolution: 2→100 Å / Num. all: 16062 / Num. obs: 16062 / % possible obs: 97.5 % |
Reflection shell | Resolution: 2→2.07 Å / % possible all: 94.76 |
Reflection | *PLUS % possible obs: 100 % / Num. measured all: 148552 / Rmerge(I) obs: 0.05 |
Reflection shell | *PLUS % possible obs: 94.8 % / Mean I/σ(I) obs: 6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1G8I Resolution: 2→19.79 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→19.79 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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