Structure analysis

Crystal structure of apo heme oxygenase-1

X-ray diffraction
2.55Å resolution
Source organism: Rattus norvegicus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10382.23 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-139216
    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
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 9960.79 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-139216
    Assembly 2
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
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 10478.9 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-139216
    Assembly 3
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

Chains: A, B, C
Length: 267 amino acids
Theoretical weight: 30.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06762 (Residues: 1-267; Coverage: 92%)
Gene name: Hmox1
Pfam: Heme oxygenase
InterPro:
CATH: Heme oxygenase-like
SCOP: Eukaryotic type heme oxygenase
PDBe-KB: UniProt Coverage View: P06762  
126720406080100120140160180200220240260
 
100200
UniProt
P06762
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Sequence conservation

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