› 2lve

X-ray diffraction
2.7Å resolution

RECOMBINANT LEN

Released:
DOI: 10.2210/pdb2lve/pdb
PDB entry 2lve coloured by chain, front view.
PDB entry 2lve coloured by chain, side view.
PDB entry 2lve coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A domain flip as a result of a single amino-acid substitution.
Pokkuluri PR, Huang DB, Raffen R, Cai X, Johnson G, Stevens PW, Stevens FJ, Schiffer M
Structure 6 1067-73 (1998)
PMID: 9739086

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138999 (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: 12.65 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P6122
Unit cell:
a: 104.4Å b: 104.4Å c: 58.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.214 0.263
Expression system: Escherichia coli

Quick links

Citations

3 review citations

An improved model of association for VH-VL immunoglobulin domains: asymmetries between VH and VL in the packing of some interface residues.
Vargas-Madrazo et al. (2003)
2 more

1 mention without citation

Site-directed mutagenesis reveals regions implicated in the stability and fiber formation of human λ3r light chains.
Villalba et al. (2015)