› 2mhm

Solution NMR

Solution structure of cytochrome c Y67H

Released:
DOI: 10.2210/pdb2mhm/pdb
PDB entry 2mhm coloured by chain, ensemble of 20 models, front view.
PDB entry 2mhm coloured by chain, ensemble of 20 models, side view.
PDB entry 2mhm coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural basis for cytochrome c Y67H mutant to function as a peroxidase.
Lan W, Wang Z, Yang Z, Ying T, Zhang X, Tan X, Liu M, Cao C, Huang ZX
PLoS One 9 e107305 (2014)
PMID: 25210769

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132226 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c isoform 1 Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 11.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P00044 (Residues: 2-109; Coverage: 99%)
Gene names: CYC1, J1653, YJR048W
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments

1 bound ligand:
Ligand HEC 1 x HEC
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 42%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions.
Hirota et al. (2018)
1 more

1 mention without citation

Structural basis for cytochrome c Y67H mutant to function as a peroxidase.
Lan et al. (2014)