› 1jfq

X-ray diffraction
1.9Å resolution

ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE ANTIBODY 36-71, "FAB 36-71"

Released:
DOI: 10.2210/pdb1jfq/pdb
PDB entry 1jfq coloured by chain, front view.
PDB entry 1jfq coloured by chain, side view.
PDB entry 1jfq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural analysis of mutants of high-affinity and low-affinity p-azophenylarsonate-specific antibodies generated by alanine scanning of heavy chain complementarity-determining region 2.
Parhami-Seren B, Viswanathan M, Strong RK, Margolies MN
J Immunol 167 5129-35 (2001)
PMID: 11673524

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134475 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig kappa chain V-V region HP 91A3 Chain: L
Molecule details ›
Chain: L
Length: 215 amino acids
Theoretical weight: 23.72 KDa
Source organism: Mus musculus
Expression system: Mus musculus
UniProt:
  • Canonical: P01648 (Residues: 1-108; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Ig heavy chain V region 36-65 Chain: H
Molecule details ›
Chain: H
Length: 222 amino acids
Theoretical weight: 23.86 KDa
Source organism: Mus musculus
Expression system: Mus musculus
UniProt:
  • Canonical: P01747 (Residues: 1-120; Coverage: 100%)
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: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 67.13Å b: 73.05Å c: 46.78Å
α: 90° β: 104.48° γ: 90°
R-values:
R R work R free
0.196 0.196 not available
Expression system: Mus musculus

Quick links

Citations

1 review citation

Detect, correct, retract: How to manage incorrect structural models.
Wlodawer et al. (2018)
2 other articles

5 mentions without citation

Multi-constraint computational design suggests that native sequences of germline antibody H3 loops are nearly optimal for conformational flexibility.
Babor et al. (2009)
4 more