› 1s5i

X-ray diffraction
2.7Å resolution

Fab (LNKB-2) of monoclonal antibody to Human Interleukin-2, crystal structure

Released:
DOI: 10.2210/pdb1s5i/pdb
PDB entry 1s5i coloured by chain, front view.
PDB entry 1s5i coloured by chain, side view.
PDB entry 1s5i coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
[A new crystal form of the Fab fragment of a monoclonal antibody to human interleukin-2: the three-dimensional structure at 2.7 A resolution].
Pletnev VZ, Goriacheva EA, Tsygannik IN, Nesmeianov VA, Pletnev SV, Pangborn W, Daux W
Bioorg Khim 30 466-9 (2004)
PMID: 15562966

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208681 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fab-fragment of monoclonal antibody Chain: L
Molecule details ›
Chain: L
Length: 219 amino acids
Theoretical weight: 24.2 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Ig gamma-1 chain C region, membrane-bound form Chain: H
Molecule details ›
Chain: H
Length: 220 amino acids
Theoretical weight: 23.87 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P01869 (Residues: 1-102; Coverage: 26%)
Gene names: Igh-4, Ighg1
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 42.816Å b: 90.682Å c: 139.819Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.2 0.275

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Citations

1 mention without citation

Three-dimensional studies of pathogenic peptides from the c-terminal of Trypanosoma cruzi ribosomal P proteins and their interaction with a monoclonal antibody structural model.
Martín et al. (2009)