Structure analysis

Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications

X-ray diffraction
1.74Å 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: 10678.98 Å2
Buried surface area: 1121.16 Å2
Dissociation area: 560.58 Å2
Dissociation energy (ΔGdiss): 12.72 kcal/mol
Dissociation entropy (TΔSdiss): 5.82 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140705
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 10743.75 Å2
Buried surface area: 1104.41 Å2
Dissociation area: 552.2 Å2
Dissociation energy (ΔGdiss): 10.6 kcal/mol
Dissociation entropy (TΔSdiss): 5.82 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140705

Macromolecules

Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09601 (Residues: 1-233; Coverage: 81%)
Gene names: HMOX1, HO, HO1
Pfam: Heme oxygenase
InterPro:
CATH: Heme oxygenase-like
SCOP: Eukaryotic type heme oxygenase

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