Brand  (β version)

PDB ID: 1LZQ

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Ligands
Code Name Style Show Link
0ZQ N-{(3s)-3-[(tert-butoxycarbonyl)amino]-4-phenylbutyl}-L-phenylalanyl-L-alpha-glutamyl-L-phenylalaninamide PoSSuM
BME Beta-mercaptoethanol PoSSuM
Non-standard Residues
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Structure summary

Code : 1LZQ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal structure of the complex of mutant HIV-1 protease (A71V, V82T, I84V) with an ethylenamine peptidomimetic inhibitor BOC-PHE-PSI[CH2CH2NH]-PHE-GLU-PHE-NH2
Release Data : 2003-04-29
Compound :
mol_id molecule chains synonym
1 PROTEASE RETROPEPSIN A,B HIV-1 PROTEASE
ec: 3.4.23.16
mutation: A71V, V82T, I84V
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 1  (taxid:11676) Escherichia coli  (taxid:562)
Authors : Skalova, T., Hasek, J., Dohnalek, J., Petrokova, H., Buchtelova, E., Soucek, M., Majer, P., Uhlikova, T., Konvalinka, J.
Keywords : HIV, PEPTIDOMIMETIC, ethylenamine ISOSTERE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

An Ethylenamine Inhibitor Binds Tightly to Both Wild Type and Mutant HIV-1 Proteases. Structure and Energy Study

Skalova, T.,Hasek, J.,Dohnalek, J.  et al.
(2003)  J.Med.Chem.  46 : 1636 - 1644

PubMed: 12699382
DOI: 10.1021/jm021079g

Reaction

Chain : A, B
UniProt : P03367 (POL_HV1BR)
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
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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 -
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 -
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 2.7.7.49 PROSITE-ProRule:PRU00405
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 2.7.7.7 PROSITE-ProRule:PRU00405
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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.