CATH Domain 3dyaA01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.10	Roll
	3.10.10	HIV Type 1 Reverse Transcriptase; Chain A, domain 1
	3.10.10.10	HIV Type 1 Reverse Transcriptase, subunit A, domain 1

Domain Context

CATH Clusters

Superfamily	HIV Type 1 Reverse Transcriptase, subunit A, domain 1
Functional Family	Gag-Pol polyprotein

Enzyme Information

2.7.7.49	RNA-directed DNA polymerase. based on mapping to UniProt P04585 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.-	Nucleotidyltransferases. based on mapping to UniProt P04585
2.7.7.7	DNA-directed DNA polymerase. based on mapping to UniProt P04585 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.-.-	Acting on ester bonds. based on mapping to UniProt P04585
3.1.13.2	Exoribonuclease H. based on mapping to UniProt P04585 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.
3.1.26.13	Retroviral ribonuclease H. based on mapping to UniProt P04585 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.
3.4.23.16	HIV-1 retropepsin. based on mapping to UniProt P04585 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)

POL_HV1H2

HIV-1 M:B_HXB2R

Gag-Pol polyprotein

PDB Structure

PDB	3DYA
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Design of annulated pyrazoles as inhibitors of HIV-1 reverse transcriptase Sweeney, Z.K., Harris, S.F., Arora, S.F., Javanbakht, H., Li, Y., Fretland, J., Davidson, J.P., Billedeau, J.R., Gleason, S.K., Hirschfeld, D., Kennedy-Smith, J.J., Mirzadegan, T., Roetz, R., Smith, M., Sperry, S., Suh, J.M., Wu, J., Tsing, S., Villasenor, A.G., Paul, A., Su, G., Heilek, G., Hang, J.Q., Zhou, A.S., Jernelius, J.A., Zhang, F.J., Klumpp, K. J.Med.Chem.