› 7xnk

Electron Microscopy
2.6Å resolution

human KCNQ1-CaM in complex with ML277

Released:
DOI: 10.2210/pdb7xnk/pdb
PDB entry 7xnk coloured by chain, front view.
PDB entry 7xnk coloured by chain, side view.
PDB entry 7xnk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanisms for the activation of human cardiac KCNQ1 channel by electro-mechanical coupling enhancers.
Ma D, Zhong L, Yan Z, Yao J, Zhang Y, Ye F, Huang Y, Lai D, Yang W, Hou P, Guo J
OpenAccess logo Proc Natl Acad Sci U S A 119 e2207067119 (2022)
PMID: 36763058
Related structures: EMD-33317

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-144007 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Potassium voltage-gated channel subfamily KQT member 1 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 692 amino acids
Theoretical weight: 76.49 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P51787 (Residues: 1-676; Coverage: 100%)
Gene names: KCNA8, KCNA9, KCNQ1, KVLQT1
Sequence domains:
Calmodulin-3 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 177 amino acids
Theoretical weight: 19.62 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P0DP25 (Residues: 1-149; Coverage: 100%)
Gene names: CALM3, CALML2, CAM3, CAMC, CAMIII
Sequence domains: EF-hand domain pair

Ligands and Environments

2 bound ligands:
Ligand K 4 x K
Ligand I0S 4 x I0S
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.6Å
Relevant EMDB volumes: EMD-33317
Expression system: Homo sapiens

Quick links

Citations

2 review citations

Recent Advances in Computer-Aided Structure-Based Drug Design on Ion Channels.
Pliushcheuskaya et al. (2023)
1 more

1 mention without citation

The membrane electric field regulates the PIP2-binding site to gate the KCNQ1 channel.
Mandala et al. (2023)