› 1b9o

X-ray diffraction
1.15Å resolution

HUMAN ALPHA-LACTALBUMIN, LOW TEMPERATURE FORM

Released:
DOI: 10.2210/pdb1b9o/pdb
PDB entry 1b9o coloured by chain, front view.
PDB entry 1b9o coloured by chain, side view.
PDB entry 1b9o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method.
Harata K, Abe Y, Muraki M
J Mol Biol 287 347-58 (1999)
PMID: 10080897

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-132931 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-lactalbumin Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 14.09 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00709 (Residues: 20-142; Coverage: 100%)
Gene names: LALBA, LYZL7
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P212121
Unit cell:
a: 33.19Å b: 49.55Å c: 64.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 not available 0.162

Quick links

Citations

1 review citation

Fluctuation matching approach for elastic network model and structure-based model of biomacromolecules.
Bope et al. (2017)
9 other articles

16 mentions without citation

The role of protein conformational fluctuations in allostery, function, and evolution.
Wrabl et al. (2011)
15 more