› 1oqh

X-ray diffraction
2.4Å resolution

Crystal Structure of the R124A mutant of the N-lobe human transferrin

Released:
DOI: 10.2210/pdb1oqh/pdb
PDB entry 1oqh coloured by chain, front view.
PDB entry 1oqh coloured by chain, side view.
PDB entry 1oqh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional consequences of binding site mutations in transferrin: crystal structures of the Asp63Glu and Arg124Ala mutants of the N-lobe of human transferrin.
Baker HM, He QY, Briggs SK, Mason AB, Baker EN
Biochemistry 42 7084-9 (2003)
PMID: 12795604

Function and Biology Details

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

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: 37.13 KDa
Source organism: Homo sapiens
Expression system: Cricetinae gen. sp.
UniProt:
  • Canonical: P02787 (Residues: 20-354; Coverage: 49%)
Gene names: PRO1400, TF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

3 bound ligands:
Ligand CO3 1 x CO3
Ligand FE 1 x FE
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 43.93Å b: 57.12Å c: 135.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.288
Expression system: Cricetinae gen. sp.

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Citations

2 review citations

Evolution of the transferrin family: conservation of residues associated with iron and anion binding.
Lambert et al. (2005)
1 more