Structure analysis

HtrA1 catalytic domain, mutationally inactivated

X-ray diffraction
2.301Å resolution
Source organism: Homo sapiens
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 26735.28 Å2
Buried surface area: 8821.42 Å2
Dissociation area: 3,003.33 Å2
Dissociation energy (ΔGdiss): 21.06 kcal/mol
Dissociation entropy (TΔSdiss): 26.1 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-187740

Macromolecules

Chains: A, B, D
Length: 231 amino acids
Theoretical weight: 25.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q92743 (Residues: 161-370; Coverage: 46%)
Gene names: HTRA, HTRA1, PRSS11
Pfam: Trypsin-like peptidase domain
InterPro:
CATH: Trypsin-like serine proteases
PDBe-KB: UniProt Coverage View: Q92743  
123120406080100120140160180200220
 
100200
UniProt
Q92743
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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