Brand  (β version)

PDB ID: 1EBK

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Ligands
Code Name Style Show Link
0Q4 N-[(2r)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamide PoSSuM
Non-standard Residues
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Structure summary

Code : 1EBK   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Structural and kinetic analysis of drug resistant mutants of HIV-1 protease
Release Data : 2000-07-26
Compound :
mol_id molecule chains
1 HIV-1 PROTEASE C,D,E,F
ec: 3.4.23.16
fragment: FRAGMENT 69-167
mutation: Q7K, R8Q, L33I, L63I, C67A, C95A
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 1  (taxid:11676) Escherichia coli  (taxid:562)
Authors : Mahalingam, B., Louis, J.M., Reed, C.C., Adomat, J.M., Krouse, J., Wang, Y.F., Harrison, R.W., Weber, I.T.
Keywords : HIV-1 PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.06 Å )
Citation :

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.

Mahalingam, B.,Louis, J.M.,Reed, C.C.  et al.
(1999)  Eur.J.Biochem.  263 : 238 - 245

PubMed: 10429209
DOI: 10.1046/j.1432-1327.1999.00514.x

Reaction

Chain : C, D, E, F
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
-
[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.