1fmb | pdb_00001fmb

EIAV PROTEASE COMPLEXED WITH THE INHIBITOR HBY-793

spinqualitylabelsall models 1fmb, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fmb is a 1 chain structure with sequence from Eiav. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HYB Activity: HIV-1 retropepsin, with EC number 3.4.23.16 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [POL_EIAVC] During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Equine infectious anemia virus (EIAV), the causative agent of infectious anemia in horses, is a member of the lentiviral family. The virus-encoded proteinase (PR) processes viral polyproteins into functional molecules during replication and it also cleaves viral nucleocapsid protein during infection. The X-ray structure of a complex of the 154G mutant of EIAV PR with the inhibitor HBY-793 was solved at 1.8 A resolution and refined to a crystallographic R-factor of 0.136. The molecule is a dimer in which the monomers are related by a crystallographic twofold axis. Although both the enzyme and the inhibitor are symmetric, the interactions between the central part of the inhibitor and the active site aspartates are asymmetric, and the inhibitor and the two flaps are partially disordered. The overall fold of EIAV PR is very similar to that of other retroviral proteinases. However, a novel feature of the EIAV PR structure is the appearance of the second alpha-helix in the monomer in a position predicted by the structural template for the family of aspartic proteinases. The parts of the EIAV PR with the highest resemblance to human immunodeficiency virus type 1 PR include the substrate-binding sites; thus, the differences in the specificity of both enzymes have to be explained by enzyme-ligand interactions at the periphery of the active site as well. Structure of equine infectious anemia virus proteinase complexed with an inhibitor.,Gustchina A, Kervinen J, Powell DJ, Zdanov A, Kay J, Wlodawer A Protein Sci. 1996 Aug;5(8):1453-65. PMID:8844837 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus protease

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