6P9B
HIV-1 Protease multiple drug resistant mutant PRS5B with 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 | HIV-1 protease | polymer | 99 | 10720.6 | 2 | UniProt (P03367) Pfam (PF00077) In PDB | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) | Retropepsin |
2 | A | {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) | |||
3 | A, B | PHOSPHATE ION | non-polymer | 95.0 | 4 | Chemie (PO4) | |||
4 | water | water | 18.0 | 121 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P03367)
PDB | External Database | Details |
---|---|---|
Lys 7 | Gln 507 | engineered mutation |
Ile 10 | Leu 510 | engineered mutation |
Ile 11 | Val 511 | engineered mutation |
Asp 21 | Glu 521 | engineered mutation |
Val 22 | Ala 522 | engineered mutation |
Met 24 | Leu 524 | engineered mutation |
Asn 35 | Glu 535 | engineered mutation |
Ile 36 | Met 536 | engineered mutation |
Asp 37 | Ser 537 | engineered mutation |
Lys 41 | Arg 541 | engineered mutation |
Leu 46 | Met 546 | engineered mutation |
Val 54 | Ile 554 | engineered mutation |
His 61 | Gln 561 | engineered mutation |
Val 62 | Ile 562 | engineered mutation |
Pro 63 | Leu 563 | engineered mutation |
Val 64 | Ile 564 | engineered mutation |
Val 66 | Ile 566 | engineered mutation |
Ala 67 | Cys 567 | engineered mutation |
Val 71 | Ala 571 | engineered mutation |
Thr 72 | Ile 572 | engineered mutation |
Thr 73 | Gly 573 | engineered mutation |
Asp 83 | Asn 583 | engineered mutation |
Val 84 | Ile 584 | engineered mutation |
Ala 95 | Cys 595 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 21441.1 | |
Non-Polymers* | Number of molecules | 5 |
Total formula weight | 885.5 | |
All* | Total formula weight | 22326.6 |