Brand  (β version)

PDB ID: 2AOI

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
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
FRD 1-phenyl-2-aminopropane
Glycosylation
Code Name Emphasize
Modification
Code Name Show
NH2 Amino group

Structure summary

Code : 2AOI   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal structure analysis of HIV-1 protease with a substrate analog P1-P6
Release Data : 2006-01-17
Compound :
mol_id molecule chains synonym
1 POL POLYPROTEIN A,B RETROPEPSIN
ec: 3.4.23.16
fragment: HIV-1 PROTEASE (RETROPEPSIN)
mutation: YES
mol_id molecule chains
2 PEPTIDE INHIBITOR C
Source :
mol_id organism_scientific expression_system
1 Human immunodeficiency virus type 1 (BH5 ISOLATE)  (taxid:11682) Escherichia coli BL21(DE3)  (taxid:469008)
strain: BH5 isolate
gene: POL
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
expression_system_plasmid: PET11A
mol_id organism_scientific
2
synthetic: yes
other_details: THIS SEQUENCE WAS CHEMICALLY SYNTHESIZED AND IS ANALOGOUS TO THE P1-P6 PROCESSING SITE IN HIV-1.
Authors : Tie, Y., Boross, P.I., Wang, Y.F., Gaddis, L., Liu, F., Chen, X., Tozser, J., Harrison, R.W., Weber, I.T.
Keywords : HIV-1 PROTEASE, MUTANT, DIMER, SUBSTRATE ANALOG, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.40 Å )
Citation :

Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.

Tie, Y.,Boross, P.I.,Wang, Y.F.  et al.
(2005)  Febs J.  272 : 5265 - 5277

PubMed: 16218957
DOI: 10.1111/j.1742-4658.2005.04923.x

Reaction

Chain : A, B
UniProt : P04587 (POL_HV1B5)
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
-
a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.49 PROSITE- ProRule:PRU00405
-
a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.7 PROSITE- ProRule:PRU00405
-