› 2brr

X-ray diffraction
1.95Å resolution

Complex of the neisserial PorA P1.4 epitope peptide and two Fab- fragments (antibody MN20B9.34)

Released:
DOI: 10.2210/pdb2brr/pdb
Model geometry
Fit model/data
PDB entry 2brr coloured by chain, front view.
PDB entry 2brr coloured by chain, side view.
PDB entry 2brr coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of an Anti-meningococcal subtype P1.4 PorA antibody provides basis for peptide-vaccine design.
Oomen CJ, Hoogerhout P, Kuipers B, Vidarsson G, van Alphen L, Gros P
J Mol Biol 351 1070-80 (2005)
PMID: 16038932

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 pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212274 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
MN20B9.34 ANTI-P1.4 ANTIBODY, FAB HEAVY CHAIN Chains: H, Y
Molecule details ›
Chains: H, Y
Length: 225 amino acids
Theoretical weight: 24.35 KDa
Source organism: Mus musculus
Expression system: Mus musculus
Structure domains: Immunoglobulins
MN20B9.34 ANTI-P1.4 ANTIBODY, FAB LIGHT CHAIN Chains: L, X
Molecule details ›
Chains: L, X
Length: 215 amino acids
Theoretical weight: 23.43 KDa
Source organism: Mus musculus
Expression system: Mus musculus
Structure domains: Immunoglobulins
Class 1 outer membrane protein variable region 2 Chain: P

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 53.666Å b: 63.833Å c: 124.701Å
α: 90° β: 86.58° γ: 90°
R-values:
R R work R free
0.2 0.198 0.238
Expression systems:
  • Mus musculus
  • Not provided

Quick links

Citations

1 review citation

History of meningococcal vaccines and their serological correlates of protection.
Vipond et al. (2012)
8 other articles

8 mentions without citation

Differential affinity of FLIP and procaspase 8 for FADD's DED binding surfaces regulates DISC assembly.
Majkut et al. (2014)
7 more