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1RTI

HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES

Summary for 1RTI
Entry DOI10.2210/pdb1rti/pdb
DescriptorHIV-1 REVERSE TRANSCRIPTASE, 1-(2-HYDROXYETHYLOXYMETHYL)-6-PHENYL THIOTHYMINE (3 entities in total)
Functional Keywordshiv-1 reverse transcriptase, nucleotidyltransferase
Biological sourceHuman immunodeficiency virus 1
More
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): P04585 P04585
Total number of polymer chains2
Total formula weight116302.35
Authors
Ren, J.,Esnouf, R.,Garman, E.,Somers, D.,Ross, C.,Kirby, I.,Keeling, J.,Darby, G.,Jones, Y.,Stuart, D.,Stammers, D. (deposition date: 1995-05-03, release date: 1996-04-03, Last modification date: 2024-10-09)
Primary citationRen, J.,Esnouf, R.,Garman, E.,Somers, D.,Ross, C.,Kirby, I.,Keeling, J.,Darby, G.,Jones, Y.,Stuart, D.
High resolution structures of HIV-1 RT from four RT-inhibitor complexes.
Nat.Struct.Biol., 2:293-302, 1995
Cited by
PubMed Abstract: We have determined the structures of four complexes of HIV-1 reverse transcriptase with non-nucleoside inhibitors, three fully refined at high resolution. The highest resolution structure is of the RT-nevirapine complex which has an R-factor of 0.186 and a root-mean-square bond length deviation of 0.015 A for all data to 2.2 A. The structures reveal a common mode of binding for these chemically diverse compounds. The common features of binding are largely hydrophobic interactions and arise from induced shape complementarity achieved by conformational rearrangement of the enzyme and conformational/configurational rearrangement of the compounds.
PubMed: 7540934
DOI: 10.1038/nsb0495-293
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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