Structure analysis

CRYSTAL AND MOLECULAR STRUCTURES OF HUMAN PROGASTRICSIN AT 1.62 ANGSTROMS RESOLUTION

X-ray diffraction
1.62Å resolution
Source organism: Homo sapiens
Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero tetramer
Accessible surface area: 27768.99 Å2
Buried surface area: 11872.45 Å2
Dissociation area: 1,290.57 Å2
Dissociation energy (ΔGdiss): -4.32 kcal/mol
Dissociation entropy (TΔSdiss): 13.97 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-148860
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 15164.13 Å2
Buried surface area: 4649.62 Å2
Dissociation area: 2,324.81 Å2
Dissociation energy (ΔGdiss): 29.17 kcal/mol
Dissociation entropy (TΔSdiss): 11.4 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-148859

Macromolecules

Chain: P
Length: 43 amino acids
Theoretical weight: 5.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20142 (Residues: 17-59; Coverage: 12%)
Gene name: PGC
Pfam: A1 Propeptide
InterPro: Aspartic peptidase, N-terminal
CATH: Helix Hairpins
SCOP: Pepsin-like
PDBe-KB: UniProt Coverage View: P20142  
143510152025303540
 
2040AVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDL
UniProt
P20142
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces

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Chain: B
Length: 329 amino acids
Theoretical weight: 35.46 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20142 (Residues: 60-388; Coverage: 88%)
Gene name: PGC
Pfam: Eukaryotic aspartyl protease
InterPro:
CATH: Acid Proteases
SCOP: Pepsin-like
PDBe-KB: UniProt Coverage View: P20142  
132950100150200250300
 
100200300
UniProt
P20142
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces

Search similar proteins