› 2rsp

X-ray diffraction
2Å resolution

STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2rsp/pdb
PDB entry 2rsp coloured by chain, front view.
PDB entry 2rsp coloured by chain, side view.
PDB entry 2rsp coloured by chain, top view.
Source organism: Rous sarcoma virus
Primary publication:
Structure of the aspartic protease from Rous sarcoma retrovirus refined at 2-A resolution.
Jaskólski M, Miller M, Rao JK, Leis J, Wlodawer A
Biochemistry 29 5889-98 (1990)
PMID: 2166563

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease p15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 13.63 KDa
Source organism: Rous sarcoma virus
Expression system: Not provided
UniProt:
  • Canonical: P03322 (Residues: 578-701; Coverage: 18%)
Gene name: gag
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 88.95Å b: 88.95Å c: 78.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.144 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Inhibitors of HIV-1 protease: a major success of structure-assisted drug design.
Wlodawer et al. (1998)
3 more

12 mentions without citation

The early years of retroviral protease crystal structures.
Miller M. (2010)
11 more