Structure analysis

Structure of the KcsA-G77C mutant or the 2,4-ion bound configuration of a K+ channel selectivity filter.

X-ray diffraction
2.13Å resolution
Assembly composition:
hetero dodecamer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dodecamer
Accessible surface area: 86400.79 Å2
Buried surface area: 37099.76 Å2
Dissociation area: 469.98 Å2
Dissociation energy (ΔGdiss): -2.47 kcal/mol
Dissociation entropy (TΔSdiss): 4.1 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-209490

Macromolecules

Chain: A
Length: 219 amino acids
Theoretical weight: 23.41 KDa
Source organism: Mus musculus
Expression system: Mammalia
InterPro:
121920406080100120140160180200
 
100200
Chains
RSRZ Outlier Chain A (auth A)
Chain A (auth A)
Domains
Secondary structure
Flexibility predictions
Ligand binding sites
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121220406080100120140160180200
 
50100150200
Chains
RSRZ Outlier Chain B (auth B)
Chain B (auth B)
Domains
Secondary structure
Flexibility predictions
Interaction interfaces

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Chain: C
Length: 103 amino acids
Theoretical weight: 11.02 KDa
Source organism: Streptomyces lividans
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A334 (Residues: 22-124; Coverage: 64%)
Gene names: kcsA, skc1
Pfam:
InterPro: Potassium channel domain
PDBe-KB: UniProt Coverage View: P0A334  
1103102030405060708090100
 
50100SALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWSVETATTVCYGDLYPVTLWGRCVAVVVMVAGITSFGLVTAALATWFVGREQERRGH
UniProt
P0A334
Chains
Domains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces

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