Brand  (β version)

PDB ID: 1DTT

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Ligands
Code Name Style Show Link
FTC N-[[3-fluoro-4-ethoxy-pyrid-2-yl]ethyl]-N'-[5-chloro-pyridyl]-thiourea PoSSuM
Non-standard Residues
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CSD 3-sulfinoalanine
Glycosylation
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Structure summary

Code : 1DTT   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/TRANSFERASE
Title : CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH PETT-2 (PETT130A94)
Release Data : 2000-04-02
Compound :
mol_id molecule chains
1 HIV-1 RT A-CHAIN A
fragment: P66
mol_id molecule chains
2 HIV-1 RT B-CHAIN B
fragment: P51
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 1  (taxid:11676) Bacteria  (taxid:2)
expression_system_common: Eubacteria
mol_id organism_scientific expression_system
2 Human immunodeficiency virus 1  (taxid:11676) Bacteria  (taxid:2)
expression_system_common: Eubacteria
Authors : Ren, J., Diprose, J., Warren, J., Esnouf, R.M., Bird, L.E., Ikemizu, S., Slater, M., Milton, J., Balzarini, J., Stuart, D.I., Stammers, D.K.
Keywords : HIV-1 reverse transcriptase AIDS, non-nucleoside inhibitor, drug design, HYDROLASE-TRANSFERASE COMPLEX
Exp. method : X-RAY DIFFRACTION ( 3.0 Å )
Citation :

Phenylethylthiazolylthiourea (PETT) non-nucleoside inhibitors of HIV-1 and HIV-2 reverse transcriptases. Structural and biochemical analyses.

Ren, J.,Diprose, J.,Warren, J.  et al.
(2000)  J.Biol.Chem.  275 : 5633 - 5639

PubMed: 10681546
DOI: 10.1074/jbc.275.8.5633

Crystallographic analysis of the binding modes of thiazoloisoindolinone non-nucleoside inhibitors to HIV-1 reverse transcriptase and comparison with modeling studies.

Ren, J.,Esnouf, R.M.,Hopkins, A.L.  et al.
(1999)  J.Med.Chem.  42 : 3845 - 3851

PubMed: 10508433
DOI: 10.1021/jm990275t

Design of MKC-442 (emivirine) analogues with improved activity against drug-resistant HIV mutants.

Hopkins, A.L.,Ren, J.,Tanaka, H.  et al.
(1999)  J.Med.Chem.  42 : 4500 - 4505

PubMed: 10579814
DOI: 10.1021/jm990192c

Crystal structures of HIV-1 reverse transcriptase in complex with carboxanilide derivatives.

Ren, J.,Esnouf, R.M.,Hopkins, A.L.  et al.
(1998)  Biochemistry  37 : 14394 - 14403

PubMed: 9772165
DOI: 10.1021/bi981309m

3'-Azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes.

Ren, J.,Esnouf, R.M.,Hopkins, A.L.  et al.
(1998)  Proc.Natl.Acad.Sci.USA  95 : 9518 - 9523

PubMed: 9689112
DOI: 10.1073/pnas.95.16.9518

Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration.

Esnouf, R.M.,Ren, J.,Garman, E.F.  et al.
(1998)  Acta Crystallogr.,Sect.D  54 : 938 - 953

PubMed: 9757109
DOI: 10.1107/S0907444998004284

Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor.

Esnouf, R.M.,Ren, J.,Hopkins, A.L.  et al.
(1997)  Proc.Natl.Acad.Sci.USA  94 : 3984 - 3989

PubMed: 9108091
DOI: 10.1073/pnas.94.8.3984

Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors.

Hopkins, A.L.,Ren, J.,Esnouf, R.M.  et al.
(1996)  J.Med.Chem.  39 : 1589 - 1600

PubMed: 8648598
DOI: 10.1021/jm960056x

The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design.

Ren, J.,Esnouf, R.,Hopkins, A.  et al.
(1995)  Structure  3 : 915 - 926

PubMed: 8535785
DOI: 10.1021/jm990275t

High resolution structures of HIV-1 RT from four RT-inhibitor complexes.

Ren, J.,Esnouf, R.,Garman, E.  et al.
(1995)  Nat.Struct.Biol.  2 : 293 - 302

PubMed: 7540934
DOI: 10.1021/jm990192c

Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors.

Esnouf, R.,Ren, J.,Ross, C.  et al.
(1995)  Nat.Struct.Biol.  2 : 303 - 308

PubMed: 7540935
DOI: 10.1021/bi981309m

Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution.

Stammers, D.K.,Somers, D.O.,Ross, C.K.  et al.
(1994)  J.Mol.Biol.  242 : 586 - 588

PubMed: 7523679
DOI: 10.1073/pnas.95.16.9518

Reaction

Chain : B
UniProt : P04585 (POL_HV1H2)
Reaction: EC: Evidence:
Physiological Direction:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. 3.4.23.16 PROSITE-ProRule:PRU00275, PubMed:32053707, PubMed:33542150
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Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. 3.1.26.13 UniProtKB:P03366
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 -
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a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.49 PROSITE- ProRule:PRU00405
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a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.7 PROSITE- ProRule:PRU00405
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