3UHL
Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20 in Complex with p2-NC substrate analog
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B, C, D | Protease | polymer | 99 | 10766.5 | 4 | UniProt (P03367) Pfam (PF00077) In PDB | Human immunodeficiency virus 1 (human) | |
2 | A, C, D | SULFATE ION | non-polymer | 96.1 | 4 | Chemie (SO4) | |||
3 | C | N-{(2S)-2-[(N-acetyl-L-threonyl-L-isoleucyl)amino]hexyl}-L-norleucyl-L-glutaminyl-N~5~-[amino(iminio)methyl]-L-ornithinamide | non-polymer | 771.0 | 1 | BIRD (PRD_000398) Chemie (2NC) | |||
4 | water | water | 18.0 | 106 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 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 | 4 |
Total formula weight | 43066.2 | |
Non-Polymers* | Number of molecules | 5 |
Total formula weight | 1155.2 | |
All* | Total formula weight | 44221.4 |