3UFN
Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20 in Complex with Saquinavir
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 | 10766.5 | 2 | UniProt (P03367) Pfam (PF00077) In PDB | Homo sapiens (human) | |
2 | A | (2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1 -phenyl-butan-2-yl]-2-(quinolin-2-ylcarbonylamino)butanediamide | non-polymer | 670.8 | 2 | BIRD (PRD_000454) Chemie (ROC) | |||
3 | B | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
4 | water | water | 18.0 | 126 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P03367)
PDB | External Database | Details |
---|---|---|
Lys 7 | Gln 507 | engineered mutation |
Phe 10 | Leu 510 | engineered mutation |
Val 13 | Ile 513 | engineered mutation |
Val 15 | Ile 515 | engineered mutation |
Asn 30 | Asp 530 | engineered mutation |
Ile 32 | Val 532 | engineered mutation |
Phe 33 | Leu 533 | engineered mutation |
Asp 35 | Glu 535 | engineered mutation |
Ile 36 | Met 536 | engineered mutation |
Asn 37 | Ser 537 | engineered mutation |
Val 47 | Ile 547 | engineered mutation |
Leu 54 | Ile 554 | engineered mutation |
Glu 58 | Gln 558 | engineered mutation |
Val 62 | Ile 562 | engineered mutation |
Pro 63 | Leu 563 | engineered mutation |
Ala 67 | Cys 567 | engineered mutation |
Val 71 | Ala 571 | engineered mutation |
Val 84 | Ile 584 | engineered mutation |
Asp 88 | Asn 588 | engineered mutation |
Thr 89 | Leu 589 | engineered mutation |
Met 90 | Leu 590 | engineered mutation |
Ala 95 | Cys 595 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 21533.1 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 1412.6 | |
All* | Total formula weight | 22945.7 |