Structure analysis

Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II

X-ray diffraction
1.65Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 11895.97 Å2
Buried surface area: 99.99 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 37.12 kcal/mol
Dissociation entropy (TΔSdiss): -0.21 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133681

Macromolecules

Chain: A
Length: 260 amino acids
Theoretical weight: 29.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Pfam: Eukaryotic-type carbonic anhydrase
InterPro:
CATH: Alpha carbonic anhydrase

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