Brand  (β version)

PDB ID: 2UY0

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Ligands
Code Name Style Show Link
HV1 Methyl [(1s)-1-({2-[(4r)-4-benzyl-4-hydroxy-5-{[(1s,2r)-2-hydroxy-2,3-dihydro-1h-inden-1-yl]amino}-5-oxopentanoyl]-2-(4-bromobenzyl)hydrazino}carbonyl)-2,2-dimethylpropyl]carbamate PoSSuM
Non-standard Residues
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Structure summary

Code : 2UY0   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Two-Carbon-Elongated HIV-1 Protease Inhibitors with a Tertiary- Alcohol-Containing Transition-State Mimic
Release Data : 2008-05-20
Compound :
mol_id molecule chains
1 HIV-1 PROTEASE A,B
ec: 3.4.23.16
fragment: RESIDUES 501-599
other_details: COMPLEX WITH INHIBITOR AHA722
Source :
mol_id organism_scientific expression_system
1 HUMAN IMMUNODEFICIENCY VIRUS 1  (taxid:11676) ESCHERICHIA COLI  (taxid:562)
strain: HIV-1 D10
variant: D10
expression_system_strain: ROSETTA
expression_system_plasmid: PET11D
Authors : Ginman, N., Samuelsson, B., Hallberg, A., Unge, J.T., Unge, T.K.
Keywords : HIV-1, PROTEASE, HYDROLASE, INHIBITOR, ASPARTYL PROTEASE
Exp. method : X-RAY DIFFRACTION ( 1.76 Å )
Citation :

Two-Carbon-Elongated HIV-1 Protease Inhibitors with a Tertiary-Alcohol-Containing Transition-State Mimic.

Wu, X.,Ohrngren, P.,Ekegren, J.K.  et al.
(2008)  J.Med.Chem.  51 : 1053

PubMed: 18215014
DOI: 10.1021/JM070680H

Reaction

Chain : A, B
UniProt : P03366 (POL_HV1B1)
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
-
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 ECO:0000250
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[Reverse transcriptase/ribonuclease H]
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 PubMed:2476069
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[Reverse transcriptase/ribonuclease H]
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 		2.7.7.49 PROSITE-ProRule:PRU00405, PubMed:2476069
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[Reverse transcriptase/ribonuclease H]
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 		2.7.7.7 PROSITE-ProRule:PRU00405, PubMed:2476069
-
Cofactor: Evidence: Note:
Mg(2+) ECO:0000250
Binds 2 magnesium ions for reverse transcriptase polymerase activity.
Mg(2+) ECO:0000250
Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.
Mg(2+) ECO:0000250
Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.