› 1b4g

Solution NMR

CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES

Released:
DOI: 10.2210/pdb1b4g/pdb
PDB entry 1b4g coloured by chain, ensemble of 22 models, front view.
PDB entry 1b4g coloured by chain, ensemble of 22 models, side view.
PDB entry 1b4g coloured by chain, ensemble of 22 models, top view.
Source organism: Homo sapiens
Primary publication:
Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate.
Antz C, Bauer T, Kalbacher H, Frank R, Covarrubias M, Kalbitzer HR, Ruppersberg JP, Baukrowitz T, Fakler B
Nat Struct Biol 6 146-50 (1999)
PMID: 10048926

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169940 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium voltage-gated channel subfamily C member 4 Chain: A
Molecule details ›
Chain: A
Length: 30 amino acids
Theoretical weight: 3.36 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q03721 (Residues: 1-30; Coverage: 5%)
Gene names: C1orf30, KCNC4
Sequence domains: Potassium voltage-gated channel

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

11 review citations

A structural interpretation of voltage-gated potassium channel inactivation.
Kurata et al. (2006)
10 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)