4JEC
Joint neutron and X-ray structure of per-deuterated HIV-1 protease in complex with clinical inhibitor amprenavir
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | HIV-1 protease | polymer | 99 | 10740.7 | 2 | UniProt (P03367) Pfam (PF00077) | Human immunodeficiency virus type 1 (HIV-1) | Protease, PR, Retropepsin |
| 2 | C (A) | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) PubChem (312) | |||
| 3 | D (B) | {3-[(4-AMINO-BENZENESULFONYL)-ISOBUTYL-AMINO]-1-BENZYL-2-HYDROXY-PROPYL}-CARBAMIC ACID TETRAHYDRO-FURAN-3-YL ESTER | non-polymer | 505.6 | 1 | Chemie (478) PubChem (2177) PubChem (22868212) PubChem (65016) PubChem (44342222) PubChem (59964701) PubChem (68088939) PubChem (68336859) PubChem (68164690) PubChem (6540587) PubChem (441385) PubChem (9898472) PubChem (92209736) PubChem (124638074) PubChem (10885665) PubChem (11168069) PubChem (141823677) | |||
| 4 | E, F (A, B) | water | water | 18.0 | 131 | Chemie (DOD) |
Sequence modifications
A, B: 1 - 99 (UniProt: P03367)
| PDB | External Database | Details |
|---|---|---|
| Lys 7 | Gln 507 | engineered mutation |
| Ile 33 | Leu 533 | engineered mutation |
| Ile 63 | Leu 563 | engineered mutation |
| Ala 67 | Cys 567 | engineered mutation |
| Ala 95 | Cys 595 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 21481.4 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 541.1 | |
| All* | Total formula weight | 22022.4 |
