Structure analysis

CARBONIC ANHYDRASE II INHIBITOR

X-ray diffraction
2.2Å 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: 11200.3 Å2
Buried surface area: 872.9 Å2
Dissociation area: 72.35 Å2
Dissociation energy (ΔGdiss): 21.69 kcal/mol
Dissociation entropy (TΔSdiss): 1.79 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133681
    Assembly 1
Confidence : 95%
No. subunits : 1
Symmetry : None
3DComplex & QSbio predictionx
No. subunits : 1
Symmetry : None
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC

Macromolecules

Chain: A
Length: 259 amino acids
Theoretical weight: 29.16 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00918 (Residues: 2-260; Coverage: 100%)
Gene name: CA2
Pfam: Eukaryotic-type carbonic anhydrase
InterPro:
CATH: Alpha carbonic anhydrase
SCOP: Carbonic anhydrase
PDBe-KB: UniProt Coverage View: P00918  
125920406080100120140160180200220240
 
100200
UniProt
P00918
Chains
Domains
Secondary structure
Flexibility predictions
Topology annotations
Early folding residue predictions
Ligand binding sites
Sequence conservation

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