Structure analysis

Calcium-loaded apo-aequorin from Aequorea victoria

X-ray diffraction
1.7Å resolution
Source organism: Aequorea victoria
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10453.89 Å2
Buried surface area: 258.5 Å2
Dissociation area: 43.67 Å2
Dissociation energy (ΔGdiss): 12.58 kcal/mol
Dissociation entropy (TΔSdiss): 0.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-139415
    Assembly 1
Confidence : 20%
No. subunits : 1
Symmetry : None
3DComplex & QSbio predictionx
No. subunits : 2
Symmetry : C2
Evidence : This biological assembly agrees with none of the predictions of PISA & EPPIC
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 17832.0 Å2
Buried surface area: 3592.81 Å2
Dissociation area: 1,537.78 Å2
Dissociation energy (ΔGdiss): 8.98 kcal/mol
Dissociation entropy (TΔSdiss): 12.6 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-139416
    Assembly 2
Confidence : 96%
No. subunits : 2
Symmetry : C2
3DComplex & QSbio predictionx
No. subunits : 2
Symmetry : C2
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC

Macromolecules

Chain: A
Length: 191 amino acids
Theoretical weight: 21.89 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P07164 (Residues: 6-196; Coverage: 97%)
Pfam:
InterPro:
CATH: EF-hand
SCOP: Calmodulin-like
PDBe-KB: UniProt Coverage View: P07164  
119120406080100120140160180
 
50100150
UniProt
P07164
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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