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1K1T

Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B
(A, B)
PROTEASE RETROPEPSINpolymer9910712.62UniProt (P04587)Human immunodeficiency virus 1
2C
(B)
N-[(2R)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamidenon-polymer833.11BIRD (PRD_000349)
Chemie (0Q4)
3D
(B)
SULFATE IONnon-polymer96.11Chemie (SO4)
4E, F
(A, B)
waterwater18.0173Chemie (HOH)
Sequence modifications
A, B: 1 - 99 (UniProt: P04587)
PDBExternal DatabaseDetails
Lys 7Gln 75engineered mutation
Ile 33Leu 101engineered mutation
Ile 45Lys 113engineered mutation
Ile 63Leu 131engineered mutation
Ala 67Cys 135engineered mutation
Ser 82Val 150engineered mutation
Ala 95Cys 163engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains2
Total formula weight21425.2
Non-Polymers*Number of molecules2
Total formula weight929.1
All*Total formula weight22354.3
*Water molecules are not included.

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PDB entries from 2026-03-25

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