› 2hrp

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
PDBe Complex ID:
PDB-CPX-225805 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
MONOCLONAL ANTIBODY F11.2.32 Chains: L, M
Molecule details ›
Chains: L, M
Length: 218 amino acids
Theoretical weight: 23.98 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
MONOCLONAL ANTIBODY F11.2.32 Chains: H, N
Molecule details ›
Chains: H, N
Length: 226 amino acids
Theoretical weight: 24.34 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
HIV-1 PROTEASE PEPTIDE Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 10 amino acids
Theoretical weight: 1.2 KDa

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 82.3Å b: 96.31Å c: 105.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.289

Quick links

Citations

5 review citations

Biologic protease inhibitors as novel therapeutic agents.
Scott et al. (2010)
4 more

7 mentions without citation

Blind prediction performance of RosettaAntibody 3.0: grafting, relaxation, kinematic loop modeling, and full CDR optimization.
Weitzner et al. (2014)
6 more