› 1efq

X-ray diffraction
1.6Å resolution

Q38D mutant of LEN

Released:
DOI: 10.2210/pdb1efq/pdb
PDB entry 1efq coloured by chain, front view.
PDB entry 1efq coloured by chain, side view.
PDB entry 1efq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Factors contributing to decreased protein stability when aspartic acid residues are in beta-sheet regions.
Pokkuluri PR, Gu M, Cai X, Raffen R, Stevens FJ, Schiffer M
Protein Sci 11 1687-94 (2002)
PMID: 12070321

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-138998 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin kappa variable 4-1 Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06312 (Residues: 21-121; Coverage: 100%)
Gene name: IGKV4-1
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
Ligand IUM 1 x IUM
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P63
Unit cell:
a: 65.8Å b: 65.8Å c: 48.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.23 0.288
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Design and Production of Bispecific Antibodies.
Wang et al. (2019)
1 more

1 mention without citation

Factors contributing to decreased protein stability when aspartic acid residues are in beta-sheet regions.
Pokkuluri et al. (2002)