Brand  (β version)

PDB ID: 1IVQ

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Ligands
Code Name Style Show Link
0PX N~1~-{(1s,2s,4s)-1-(cyclohexylmethyl)-4-[(2,2-dimethylpropyl)carbamoyl]-2-hydroxy-5-methylhexyl}-N~2~-(quinolin-2-ylcar bonyl)-L-aspartamide PoSSuM
Non-standard Residues
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Structure summary

Code : 1IVQ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : THE CRYSTALLOGRAPHIC STRUCTURE OF THE PROTEASE FROM HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 WITH TWO SYNTHETIC PEPTIDIC TRANSITION STATE ANALOG INHIBITORS
Release Data : 1993-07-15
Compound :
mol_id molecule chains
1 HIV-2 PROTEASE A,B
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 2  (taxid:11709) Escherichia coli  (taxid:562)
Authors : Mulichak, A.M., Watenpaugh, K.D.
Keywords : ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.6 Å )
Citation :

The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors.

Mulichak, A.M.,Hui, J.O.,Tomasselli, A.G.  et al.
(1993)  J.Biol.Chem.  268 : 13103 - 13109

PubMed: 8514751

Reaction

Chain : A, B
UniProt : P04584 (POL_HV2RO)
Reaction: EC: Evidence:
Physiological Direction:
Endopeptidase for which the P1 residue is preferably hydrophobic. 3.4.23.47 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 ECO:0000250
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 ECO:0000250
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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.