› 6duj

X-ray diffraction
1.82Å resolution

Crystal structure of A51V variant of Human Cytochrome c

Released:
DOI: 10.2210/pdb6duj/pdb
PDB entry 6duj coloured by chain, front view.
PDB entry 6duj coloured by chain, side view.
PDB entry 6duj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity.
Lei H, Bowler BE
J Phys Chem B 123 8939-8953 (2019)
PMID: 31557440

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-161387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c Chains: A, C
Molecule details ›
Chains: A, C
Length: 104 amino acids
Theoretical weight: 11.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P99999 (Residues: 2-105; Coverage: 99%)
Gene names: CYC, CYCS
Sequence domains: Cytochrome c

Ligands and Environments

1 bound ligand:
Ligand HEC 2 x HEC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 62.38Å b: 184.369Å c: 35.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.184 0.235
Expression system: Escherichia coli

Quick links

Citations

1 review citation

In Situ Spectroelectrochemical Investigations of Electrode-Confined Electron-Transferring Proteins and Redox Enzymes.
Murgida DH. (2021)
7 other articles

1 mention without citation

Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity.
Lei et al. (2019)