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

Summary for 1K2C

Related1A8K 1A94 1DW6 1DAZ 1K1T 1K1U 1K2B
Related PRD IDPRD_000349
DescriptorPROTEASE RETROPEPSIN, N-[(2R)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamide (3 entities in total)
Functional Keywordshiv-1 protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Cellular locationMatrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential) P04587
Total number of polymer chains2
Total molecular weight22288.33
Mahalingam, B.,Boross, P.,Wang, Y.-F.,Louis, J.M.,Fischer, C.,Tozser, J.,W Harrison, R.,Weber, I.T. (deposition date: 2001-09-26, release date: 2002-07-10, Last modification date: 2012-12-12)
Primary citation
Mahalingam, B.,Boross, P.,Wang, Y.F.,Louis, J.M.,Fischer, C.C.,Tozser, J.,Harrison, R.W.,Weber, I.T.
Combining mutations in HIV-1 protease to understand mechanisms of resistance.
Proteins, 48:107-116, 2002
PubMed: 12012342 (PDB entries with the same primary citation)
DOI: 10.1002/prot.10140
MImport into Mendeley
Experimental method
NMR Information

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.3031006.8%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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