› 1byw

X-ray diffraction
2.6Å resolution

STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL

Released:
DOI: 10.2210/pdb1byw/pdb
PDB entry 1byw coloured by chain, front view.
PDB entry 1byw coloured by chain, side view.
PDB entry 1byw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain.
Morais Cabral JH, Lee A, Cohen SL, Chait BT, Li M, Mackinnon R
Cell 95 649-55 (1998)
PMID: 9845367

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium voltage-gated channel subfamily H member 2 Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12809 (Residues: 26-135; Coverage: 10%)
Gene names: ERG, ERG1, HERG, KCNH2
Sequence domains: PAS domain
Structure domains: PAS domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P6522
Unit cell:
a: 56.1Å b: 56.1Å c: 135.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.252 0.252 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

78 review citations

PAS domains: internal sensors of oxygen, redox potential, and light.
Taylor et al. (1999)
77 more

25 mentions without citation

Structure and signaling mechanism of Per-ARNT-Sim domains.
Möglich et al. (2009)
24 more