7n4f

X-ray diffraction
1.8Å resolution

Ni-bound crystal structure of the engineered cyt cb562 variant, AB2-H100A, crystallized in the presence of Ni(II)

Released:
Model geometry
Fit model/data
Source organism: Escherichia coli
Primary publication:
Overcoming universal restrictions on metal selectivity by protein design.
Nature 603 522-527 (2022)
PMID: 35236987

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-142156 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble cytochrome b562 Chains: A, C
Molecule details ›
Chains: A, C
Length: 106 amino acids
Theoretical weight: 11.85 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABE7 (Residues: 23-128; Coverage: 100%)
Gene name: cybC
Sequence domains: Cytochrome b562

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 34.47Å b: 84.65Å c: 39.14Å
α: 90° β: 100.51° γ: 90°
R-values:
R R work R free
0.212 0.208 0.254
Expression system: Escherichia coli