› 1m20

X-ray diffraction
1.8Å resolution

Crystal Structure of F35Y Mutant of Trypsin-solubilized Fragment of Cytochrome b5

Released:
DOI: 10.2210/pdb1m20/pdb
PDB entry 1m20 coloured by chain, front view.
PDB entry 1m20 coloured by chain, side view.
PDB entry 1m20 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35-->Tyr mutant.
Yao P, Wu J, Wang YH, Sun BY, Xia ZX, Huang ZX
Eur J Biochem 269 4287-96 (2002)
PMID: 12199707

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome b5 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.49 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00171 (Residues: 8-89; Coverage: 61%)
Gene names: CYB5, CYB5A
Sequence domains: Cytochrome b5-like Heme/Steroid binding domain
Structure domains: Cytochrome b5-like heme/steroid binding domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 70.709Å b: 40.388Å c: 39.299Å
α: 90° β: 111.72° γ: 90°
R-values:
R R work R free
0.193 0.193 0.227
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

A Protein Structure Initiative approach to expression, purification, and in situ delivery of human cytochrome b5 to membrane vesicles.
Sobrado et al. (2008)
5 more

1 mention without citation

Experimental Studies on MoS2-Treated Grinding Wheel Active Surface Condition after High-Efficiency Internal Cylindrical Grinding Process of INCONEL® Alloy 718.
Kapłonek et al. (2019)