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Electron Microscopy
2.7Å resolution

Human erythrocyte catalase

Released:
Source organism: Homo sapiens
Primary publication:
Factors affecting macromolecule orientations in thin films formed in cryo-EM.
OpenAccess logo Acta Crystallogr D Struct Biol (2024)
PMID: 38935342
Related structures: EMD-37954

Function and Biology Details

Reaction catalysed:
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 527 amino acids
Theoretical weight: 59.84 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P04040 (Residues: 1-527; Coverage: 100%)
Gene name: CAT
Sequence domains:

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.7Å
Relevant EMDB volumes: EMD-37954