Structure analysis

Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1

X-ray diffraction
1.88Å 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: 10714.1 Å2
Buried surface area: 1005.23 Å2
Dissociation area: 502.61 Å2
Dissociation energy (ΔGdiss): 11.71 kcal/mol
Dissociation entropy (TΔSdiss): 5.82 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140705
    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: 10671.55 Å2
Buried surface area: 1031.7 Å2
Dissociation area: 515.85 Å2
Dissociation energy (ΔGdiss): 11.31 kcal/mol
Dissociation entropy (TΔSdiss): 5.82 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140705
    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

Macromolecules

Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.91 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
PDBe-KB: UniProt Coverage View: P09601  
123320406080100120140160180200220
 
100200
UniProt
P09601
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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