› 3fgs

X-ray diffraction
1.8Å resolution

Crystal structure of G65R/K206E double mutant of the N-lobe human transferrin

Released:
DOI: 10.2210/pdb3fgs/pdb
PDB entry 3fgs coloured by chain, front view.
PDB entry 3fgs coloured by chain, side view.
PDB entry 3fgs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional consequences of the substitution of glycine 65 with arginine in the N-lobe of human transferrin.
Mason AB, Halbrooks PJ, James NG, Byrne SL, Grady JK, Chasteen ND, Bobst CE, Kaltashov IA, Smith VC, MacGillivray RT, Everse SJ
Biochemistry 48 1945-53 (2009)
PMID: 19219998

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serotransferrin Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 37.32 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P02787 (Residues: 20-356; Coverage: 50%)
Gene names: PRO1400, TF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand CO3 1 x CO3
Ligand FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 43.347Å b: 57.056Å c: 133.737Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.246
Expression system: Mesocricetus auratus

Quick links

Citations

2 review citations

Molecular mechanisms of disease-causing missense mutations.
Stefl et al. (2013)
1 more

1 mention without citation

Structural and functional consequences of the substitution of glycine 65 with arginine in the N-lobe of human transferrin.
Mason et al. (2009)