3TTP
Structure of multiresistant HIV-1 protease in complex with darunavir
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 | 10822.7 | 2 | UniProt (P03367) Pfam (PF00077) In PDB | Human immunodeficiency virus type 1 (HIV-1) | |
2 | A | (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE | non-polymer | 547.7 | 1 | Chemie (017) | |||
3 | A, B | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
4 | A | BETA-MERCAPTOETHANOL | non-polymer | 78.1 | 1 | Chemie (BME) | |||
5 | water | water | 18.0 | 68 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P03367)
PDB | External Database | Details |
---|---|---|
Val 13 | Ile 513 | engineered mutation |
Arg 20 | Lys 520 | 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 |
Lys 41 | Arg 541 | engineered mutation |
Thr 43 | Lys 543 | engineered mutation |
Val 47 | Ile 547 | engineered mutation |
Met 54 | Ile 554 | engineered mutation |
Val 62 | Ile 562 | engineered mutation |
Val 63 | Leu 563 | engineered mutation |
Val 71 | Ala 571 | engineered mutation |
Thr 72 | Ile 572 | engineered mutation |
Ser 73 | Gly 573 | engineered mutation |
Pro 74 | Thr 574 | engineered mutation |
Leu 82 | Val 582 | engineered mutation |
Val 89 | Leu 589 | engineered mutation |
Leu 93 | Ile 593 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 21645.3 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 696.7 | |
All* | Total formula weight | 22342.0 |