Brand  (β version)

PDB ID: 1IDA

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Ligands
Code Name Style Show Link
0PO N-[(1r)-1-{[(1s,2s)-1-benzyl-3-{(2r,4s)-2-(tert-butylcarbamoyl)-4-[(pyridin-3-ylmethyl)sulfanyl]piperidin-1-yl}-2-hydroxypropyl]carbamoyl}-2-methylpropyl]quinoline-2-carboxamide PoSSuM
Non-standard Residues
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Structure summary

Code : 1IDA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : CRYSTAL STRUCTURES OF HIV-2 PROTEASE IN COMPLEX WITH INHIBITORS CONTAINING THE HYDROXYETHYLAMINE DIPEPTIDE ISOSTERE
Release Data : 1995-01-26
Compound :
mol_id molecule chains synonym
1 Protease A,B Retropepsin, PR
ec: 3.4.23.47
fragment: rsidues 514-622
Source :
mol_id organism_scientific organism_common expression_system
1 Human immunodeficiency virus type 2  (taxid:11709) HIV-2 Escherichia coli  (taxid:562)
gene: gag-pol
Authors : Tong, L., Anderson, P.C.
Keywords : ACID PROTEINASE, AIDS, Protease, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.7 Å )
Citation :

Crystal structures of HIV-2 protease in complex with inhibitors containing the hydroxyethylamine dipeptide isostere.

Tong, L.,Pav, S.,Mui, S.  et al.
(1995)  Structure  3 : 33 - 40

PubMed: 7743130
DOI: 10.1016/S0969-2126(01)00133-2

Crystal Structure of Human Immunodeficiency Virus (HIV) Type 2 Protease in Complex with a Reduced Amide Inhibitor and Comparison with HIV-1 Protease Structures

Tong, L.,Pav, S.,Pargellis, C.  et al.
(1993)  Proc.Natl.Acad.Sci.USA  90 : 8387

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
-
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.