Brand  (β version)

PDB ID: 3EL9

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
ACT Acetate ion PoSSuM
DR7 (3s,8s,9s,12s)-3,12-bis(1,1-dimethylethyl)-8-hydroxy-4,11-dioxo-9-(phenylmethyl)-6-[[4-(2-pyridinyl)phenyl]methyl]-2,5, 6,10,13-pentaazatetradecanedioic acid dimethyl ester PoSSuM
PO4 Phosphate ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 3EL9   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of atazanavir (ATV) in complex with a multidrug HIV-1 protease (V82T/I84V)
Release Data : 2009-09-01
Compound :
mol_id molecule chains synonym
1 Protease A,B Retropepsin, PR
ec: 3.4.23.16
fragment: UNP residues 484-582
mutation: Q7K, V82T, I84V
Source :
mol_id organism_scientific organism_common expression_system
1 HIV-1 M:B_ARV2/SF2  (taxid:11685) HIV-1 Escherichia coli  (taxid:562)
strain: HXB2
gene: gag-pol
expression_system_strain: TAP106
expression_system_vector_type: PXC35
expression_system_plasmid: pEN
Authors : Prabu-Jeyabalan, M., King, N., Schiffer, C.
Keywords : drug resistance, entropy enthalpy compensation, hiv protease, atazanavir, AIDS, Hydrolase
Exp. method : X-RAY DIFFRACTION ( 1.60 Å )
Citation :

Extreme Entropy-Enthalpy Compensation in a Drug-Resistant Variant of HIV-1 Protease.

King, N.M.,Prabu-Jeyabalan, M.,Bandaranayake, R.M.  et al.
(2012)  Acs Chem.Biol.  7 : 1536 - 1546

PubMed: 22712830
DOI: 10.1021/cb300191k

Reaction

Chain : A, B
UniProt : P03369 (POL_HV1A2)
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
-
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
-
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 3.1.13.2 ECO:0000250
-
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 2.7.7.49 PROSITE-ProRule:PRU00405
-
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 2.7.7.7 PROSITE-ProRule:PRU00405
-
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.