› 3eyc

X-ray diffraction
2.6Å resolution

New crystal structure of human tear lipocalin in complex with 1,4-butanediol in space group P21

Released:
DOI: 10.2210/pdb3eyc/pdb
PDB entry 3eyc coloured by chain, front view.
PDB entry 3eyc coloured by chain, side view.
PDB entry 3eyc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavity.
Breustedt DA, Chatwell L, Skerra A
Acta Crystallogr D Biol Crystallogr 65 1118-25 (2009)
PMID: 19770509

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151894 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipocalin-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 162 amino acids
Theoretical weight: 17.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31025 (Residues: 23-176; Coverage: 98%)
Gene names: LCN1, VEGP
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand BU1 4 x BU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 63.907Å b: 34.166Å c: 143.481Å
α: 90° β: 90.35° γ: 90°
R-values:
R R work R free
0.228 0.228 0.274
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The international workshop on meibomian gland dysfunction: report of the subcommittee on tear film lipids and lipid-protein interactions in health and disease.
Green-Church et al. (2011)
5 more

10 mentions without citation

Focus on molecules: tear lipocalin.
Glasgow et al. (2011)
9 more