1Z1H
HIV-1 protease complexed with macrocyclic peptidomimetic inhibitor 3
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B | d1z1hb1 | All beta proteins | Acid proteases | Acid proteases | Retroviral protease (retropepsin) | Human immunodeficiency virus type 1 protease | ( ) [TaxId: ], (Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) ) [TaxId: 11685 ], | SCOPe (2.08) |
A | d1z1ha1 | All beta proteins | Acid proteases | Acid proteases | Retroviral protease (retropepsin) | Human immunodeficiency virus type 1 protease | ( ) [TaxId: ], (Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) ) [TaxId: 11685 ], | SCOPe (2.08) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B | RVP | e1z1hB1 | A: beta barrels | X: cradle loop barrel | H: RIFT-related | T: acid protease | F: RVP | ECOD (1.6) |
A | RVP | e1z1hA1 | A: beta barrels | X: cradle loop barrel | H: RIFT-related | T: acid protease | F: RVP | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
B | 2.40.70.10 | Mainly Beta | Beta Barrel | Cathepsin D, subunit A | domain 1 | CATH (4.3.0) |
A | 2.40.70.10 | Mainly Beta | Beta Barrel | Cathepsin D, subunit A | domain 1 | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00077 | Retroviral aspartyl protease (RVP) | Retroviral aspartyl protease | Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a ... | Domain |