› 1qac

X-ray diffraction
1.8Å resolution

CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE

Released:
DOI: 10.2210/pdb1qac/pdb
PDB entry 1qac coloured by chain, front view.
PDB entry 1qac coloured by chain, side view.
PDB entry 1qac coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface.
Pokkuluri PR, Cai X, Johnson G, Stevens FJ, Schiffer M
Protein Sci 9 1852-5 (2000)
PMID: 11045631

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 Chains: A, B
Molecule details ›
Chains: A, B
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 35.3Å b: 83.6Å c: 42.8Å
α: 90° β: 109° γ: 90°
R-values:
R R work R free
0.193 0.193 0.226
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers.
Rossmann et al. (2011)
2 more

2 mentions without citation

Malachite green mediates homodimerization of antibody VL domains to form a fluorescent ternary complex with singular symmetric interfaces.
Szent-Gyorgyi et al. (2013)
1 more