› 2dlf

X-ray diffraction
1.55Å resolution

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE FV FRAGMENT FROM AN ANTI-DANSYL SWITCH VARIANT ANTIBODY IGG2A(S) CRYSTALLIZED AT PH 6.75

Released:
DOI: 10.2210/pdb2dlf/pdb
Model geometry
Fit model/data
PDB entry 2dlf coloured by chain, front view.
PDB entry 2dlf coloured by chain, side view.
PDB entry 2dlf coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The pH-dependent structural variation of complementarity-determining region H3 in the crystal structures of the Fv fragment from an anti-dansyl monoclonal antibody.
Nakasako M, Takahashi H, Shimba N, Shimada I, Arata Y
J Mol Biol 291 117-34 (1999)
PMID: 10438610

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134457 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig kappa chain V-II region 26-10 Chain: L
Molecule details ›
Chain: L
Length: 113 amino acids
Theoretical weight: 12.39 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P01631 (Residues: 1-113; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Ig heavy chain V-III region J606 Chain: H
Molecule details ›
Chain: H
Length: 124 amino acids
Theoretical weight: 14.15 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P01801 (Residues: 1-99, 100-101, 102-115; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P212121
Unit cell:
a: 57.29Å b: 66.93Å c: 53.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.233

Quick links

Citations

1 review citation

Approaches to efficiently estimate solvation and explicit water energetics in ligand binding: the use of WaterMap.
Yang et al. (2013)
10 other articles

5 mentions without citation

Probability-based protein secondary structure identification using combined NMR chemical-shift data.
Wang et al. (2002)
4 more