› 5mhh

X-ray diffraction
2Å resolution

Crystal structure of engineered human lipocalin 2 carrying p-boronophenylalanine at position 36

Released:
DOI: 10.2210/pdb5mhh/pdb
PDB entry 5mhh coloured by chain, front view.
PDB entry 5mhh coloured by chain, side view.
PDB entry 5mhh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Rational Design of an Anticalin-Type Sugar-Binding Protein Using a Genetically Encoded Boronate Side Chain.
Edwardraja S, Eichinger A, Theobald I, Sommer CA, Reichert AJ, Skerra A
ACS Synth Biol 6 2241-2247 (2017)
PMID: 28937743

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-160356 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil gelatinase-associated lipocalin Chain: A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 21.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P80188 (Residues: 21-198; Coverage: 100%)
Gene names: HNL, LCN2, NGAL
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand 7N8 1 x 7N8

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I4
Unit cell:
a: 90.857Å b: 90.857Å c: 44.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.233
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Future prospects for noncanonical amino acids in biological therapeutics.
Rezhdo et al. (2019)
1 more

1 mention without citation

A Tetrahedral Boronic Acid Diester Formed by an Unnatural Amino Acid in the Ligand Pocket of an Engineered Lipocalin.
Sommer et al. (2020)