Structure analysis

X-RAY ANALYSES OF ASPARTIC PROTEASES. II. THREE-DIMENSIONAL STRUCTURE OF THE HEXAGONAL CRYSTAL FORM OF PORCINE PEPSIN AT 2.3 ANGSTROMS RESOLUTION

X-ray diffraction
2.34Å resolution
Source organism: Sus scrofa
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 13453.02 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133553
    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: 326 amino acids
Theoretical weight: 34.47 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00791 (Residues: 60-385; Coverage: 88%)
Gene name: PGA
Pfam: Eukaryotic aspartyl protease
InterPro:
CATH: Acid Proteases
SCOP: Pepsin-like
PDBe-KB: UniProt Coverage View: P00791  
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