CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family Gag-Pol polyprotein

Enzyme Information

2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P0C6F2
2.7.7.49
RNA-directed DNA polymerase.
based on mapping to UniProt P0C6F2
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
-!- Catalyzes RNA-template-directed extension of the 3'-end of a DNA strand by one deoxynucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a RNA or DNA primer. -!- DNA can also serve as template. -!- See also EC 2.7.7.7.
2.7.7.7
DNA-directed DNA polymerase.
based on mapping to UniProt P0C6F2
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
-!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49.
3.1.26.13
Retroviral ribonuclease H.
based on mapping to UniProt P0C6F2
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.
-!- Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication. -!- To perform this task the enzyme combines two distinct activities. -!- The polymerase domain (EC 2.7.7.49) occupies the N-terminal two- thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third. -!- The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites.
3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P0C6F2
3.1.13.2
Exoribonuclease H.
based on mapping to UniProt P0C6F2
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
-!- This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13.
3.4.23.16
HIV-1 retropepsin.
based on mapping to UniProt P0C6F2
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
-!- Present in human immunodeficiency virus type 1. -!- Contributes to the maturation of the viral particle, and is a target of antiviral drugs. -!- Active enzyme is a dimer of identical 11-kDa subunits. -!- Similar enzymes occur in other retroviruses. -!- Belongs to peptidase family A2.

UniProtKB Entries (1)

P0C6F2
POL_HV1LW
Human immunodeficiency virus type 1 lw12.3 isolate
Gag-Pol polyprotein

PDB Structure

PDB 4MC6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Optimization of Cyclic Sulfonamide based Novel HIV-1 Protease Inhibitors to Pico Molar Affinities guided by X-ray Crystallographic Analysis
Ganguly, A.K., Alluri, S.S., Wang, C.H., Antropow, A., White, A., Caroccia, D., Biswas, D., Kang, E., Zhang, L.K., Carroll, S.S., Burlein, C., Fay, J., Orth, P., Strickland, C.
Tetrahedron