› 1lfh

X-ray diffraction
2.8Å resolution

MOLECULAR REPLACEMENT SOLUTION OF THE STRUCTURE OF APOLACTOFERRIN, A PROTEIN DISPLAYING LARGE-SCALE CONFORMATIONAL CHANGE

Released:
DOI: 10.2210/pdb1lfh/pdb
PDB entry 1lfh coloured by chain, front view.
PDB entry 1lfh coloured by chain, side view.
PDB entry 1lfh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change.
Norris GE, Anderson BF, Baker EN
Acta Crystallogr B 47 ( Pt 6) 998-1004 (1991)
PMID: 1772635

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactotransferrin Chain: A
Molecule details ›
Chain: A
Length: 691 amino acids
Theoretical weight: 76.22 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02788 (Residues: 20-710; Coverage: 100%)
Gene names: GIG12, LF, LTF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 152.09Å b: 94.58Å c: 55.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 not available not available
Expression system: Not provided

Quick links

Citations

1 review citation

Normal mode analysis and applications in biological physics.
Dykeman et al. (2010)
13 other articles

24 mentions without citation

Normal-modes-based prediction of protein conformational changes guided by distance constraints.
Zheng et al. (2005)
23 more