Brand  (β version)

PDB ID: 2IEO

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
017 (3r,3as,6ar)-hexahydrofuro[2,3-B]furan-3-yl(1s,2r)-3-[[(4-aminophenyl)sulfonyl](isobutyl)amino]-1-benzyl-2-hydroxypropylcarbamate PoSSuM
CL Chloride ion PoSSuM
NA Sodium ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 2IEO   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure analysis of HIV-1 protease mutant I84V with a potent non-peptide inhibitor (UIC-94017)
Release Data : 2006-10-03
Compound :
mol_id molecule chains synonym
1 Protease A,B RETROPEPSIN
ec: 3.4.23.16
fragment: residues 500-598
mutation: Q7K, L33I, L63I, C67A, I84V, C95A, Q107K, L133I, L163I, C167A, C195A
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus 1  (taxid:11676) Escherichia coli BL21(DE3)  (taxid:469008)
gene: gag, pol
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
expression_system_plasmid: PET11A
Authors : Tie, Y., Boross, P.I., Wang, Y.F., Gaddis, L., Manna, D., Hussain, A.K., Leshchenko, S., Ghosh, A.K., Louis, J.M., Harrison, R.W., Weber, I.T.
Keywords : HIV-1 protease, mutant, I84V, dimer, inhibitor, UIC-94017, TMC114, darunavir, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.53 Å )
Citation :

High Resolution Crystal Structures of HIV-1 Protease with a Potent Non-Peptide Inhibitor (Uic-94017) Active Against Multi-Drug-Resistant Clinical Strains.

Tie, Y.,Boross, P.I.,Wang, Y.F.  et al.
(2004)  J.Mol.Biol.  338 : 341 - 352

PubMed: 15066436
DOI: 10.1016/j.jmb.2004.02.052

Reaction

Chain : A, B
UniProt : P03368 (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
-
[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
-
[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.