DB code: M00166

RLCP classification 1.13.200.966 : Hydrolysis
3.103.90021.1120 : Transfer
CATH domain 1.10.150.90 : DNA polymerase; domain 1
1.10.375.- : Human Immunodeficiency Virus Type 1 Capsid Protein
1.10.1200.- : Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A
4.10.60.- : HIV-1 Nucleocapsid Protein
-.-.-.- :
2.40.70.10 : Cathepsin D, subunit A; domain 1 Catalytic domain
-.-.-.- :
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1
3.30.70.270 : Alpha-Beta Plaits Catalytic domain
3.30.70.270 : Alpha-Beta Plaits
3.30.70.270 : Alpha-Beta Plaits
3.30.420.10 : Nucleotidyltransferase; domain 5 Catalytic domain
1.10.10.200 : Arc Repressor Mutant, subunit A
3.30.420.10 : Nucleotidyltransferase; domain 5
2.30.30.- : SH3 type barrels.
-.-.-.- :
E.C. 3.4.23.47 2.7.7.49 2.7.7.7 3.1.26.4
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.10.200 : Arc Repressor Mutant, subunit A M00206
2.40.70.10 : Cathepsin D, subunit A; domain 1 D00471 D00436 D00438 D00439 D00440 D00441 D00442 D00443 D00437 D00444 D00423 D00445 D00484 M00206 D00231 D00529
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1 M00206 M00135 M00146
3.30.420.10 : Nucleotidyltransferase; domain 5 M00206 T00252 M00019 M00020 M00055 M00135 M00146 M00173 M00175 M00186
3.30.70.270 : Alpha-Beta Plaits M00206 M00019 M00135 M00146 M00209

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains Pfam
P04584 Gag-Pol polyprotein
Pr160Gag-Pol
Matrix protein p17
(MA)
Capsid protein p24
(CA)
Spacer peptide p2
Nucleocapsid protein p7
(NC)
Transframe peptide
(TF)
p6-pol
(p6*)
Protease
EC 3.4.23.47
PR Retropepsin
Reverse transcriptase/ribonuclease H
EC 2.7.7.49
EC 2.7.7.7
EC 3.1.26.13
Exoribonuclease H
EC 3.1.13.2
p66 RT
p51 RT
p15
Integrase
(IN)
PF00540 (Gag_p17)
PF00607 (Gag_p24)
PF00552 (IN_DBD_C)
PF02022 (Integrase_Zn)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
PF06815 (RVT_connect)
PF06817 (RVT_thumb)
PF00098 (zf-CCHC)
[Graphical View]

KEGG enzyme name
HIV-2 retropepsin
(EC 3.4.23.47 )
RNA-directed DNA polymerase
(EC 2.7.7.49 )
DNA nucleotidyltransferase (RNA-directed)
(EC 2.7.7.49 )
reverse transcriptase
(EC 2.7.7.49 )
revertase
(EC 2.7.7.49 )
RNA-dependent deoxyribonucleate nucleotidyltransferase
(EC 2.7.7.49 )
RNA revertase
(EC 2.7.7.49 )
RNA-dependent DNA polymerase
(EC 2.7.7.49 )
RNA-instructed DNA polymerase
(EC 2.7.7.49 )
RT
(EC 2.7.7.49 )
DNA-directed DNA polymerase
(EC 2.7.7.7 )
DNA polymerase I
(EC 2.7.7.7 )
DNA polymerase II
(EC 2.7.7.7 )
DNA polymerase III
(EC 2.7.7.7 )
DNA polymerase alpha
(EC 2.7.7.7 )
DNA polymerase beta
(EC 2.7.7.7 )
DNA polymerase gamma
(EC 2.7.7.7 )
DNA nucleotidyltransferase (DNA-directed)
(EC 2.7.7.7 )
DNA nucleotidyltransferase (DNA-directed)
(EC 2.7.7.7 )
deoxyribonucleate nucleotidyltransferase
(EC 2.7.7.7 )
deoxynucleate polymerase
(EC 2.7.7.7 )
deoxyribonucleic acid duplicase
(EC 2.7.7.7 )
deoxyribonucleic acid polymerase
(EC 2.7.7.7 )
deoxyribonucleic duplicase
(EC 2.7.7.7 )
deoxyribonucleic polymerase
(EC 2.7.7.7 )
deoxyribonucleic polymerase I
(EC 2.7.7.7 )
DNA duplicase
(EC 2.7.7.7 )
DNA nucleotidyltransferase
(EC 2.7.7.7 )
DNA polymerase
(EC 2.7.7.7 )
DNA replicase
(EC 2.7.7.7 )
DNA-dependent DNA polymerase
(EC 2.7.7.7 )
duplicase
(EC 2.7.7.7 )
Klenow fragment
(EC 2.7.7.7 )
sequenase
(EC 2.7.7.7 )
Taq DNA polymerase
(EC 2.7.7.7 )
Taq Pol I
(EC 2.7.7.7 )
Tca DNA polymerase
(EC 2.7.7.7 )
calf thymus ribonuclease H
(EC 3.1.26.4 )
endoribonuclease H (calf thymus)
(EC 3.1.26.4 )
RNase H
(EC 3.1.26.4 )
RNA*DNA hybrid ribonucleotidohydrolase
(EC 3.1.26.4 )
hybrid ribonuclease
(EC 3.1.26.4 )
hybridase
(EC 3.1.26.4 )
hybridase (ribonuclease H)
(EC 3.1.26.4 )
ribonuclease H
(EC 3.1.26.4 )
hybrid nuclease
(EC 3.1.26.4 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P04584 POL_HV2RO Endonucleolytic cleavage to 5''- phosphomonoester. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Endopeptidase for which the P1 residue is preferably hydrophobic. Matrix protein p17 is a trimer. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. The integrase is a homodimer and possibly a homotetramer (By similarity). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential). Nucleus (Potential). Cytoplasm (Potential). Note=Nuclear at initial phase, cytoplasmic at assembly (Potential). Matrix protein p17: Virion (Potential). Nucleus (By similarity). Cytoplasm (By similarity). Cell membrane, Lipid-anchor (Potential). Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Binds 2 magnesium ions for reverse transcriptase polymerase activity (By similarity). Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding (By similarity). Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions (By similarity).

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism 2.7.7.7
MAP00240 Pyrimidine metabolism 2.7.7.7

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00038 C00017 C00012 C00677 C00039 C00046 C00001 C00017 C00012 C00013 C00039 C00960 I00136
E.C. 2.7.7.49
2.7.7.7
3.1.26.4
3.4.23.47
3.4.23.47
2.7.7.49
2.7.7.7
2.7.7.49
2.7.7.7
3.1.26.4
3.1.26.4
3.4.23.47
3.4.23.47
3.4.23.47
2.7.7.49
2.7.7.7
2.7.7.49
2.7.7.7
3.1.26.4
3.4.23.47
Compound Magnesium Zinc Protein Peptide Deoxynucleoside triphosphate DNA(n) RNA H2O Protein Peptide Pyrophosphate DNA(n+1) RNA 5'-phosphate Amino-diol-tetrahedral intermediate
Type divalent metal (Ca2+, Mg2+) heavy metal peptide/protein peptide/protein nucleotide nucleic acids nucleic acids H2O peptide/protein peptide/protein phosphate group/phosphate ion nucleic acids nucleic acids,phosphate group/phosphate ion
ChEBI 18420
18420
29105
29105
15377
15377
29888
29888
PubChem 888
888
32051
32051
22247451
962
22247451
962
1023
21961011
1023
21961011
1hiiA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:C20
1hshA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:MK1
1hshC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:MK1
1hsiA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1idaA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:0PO
1idbA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:0DO
1ivpA Unbound Unbound Unbound Analogue:1ZK Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ivqA Unbound Unbound Unbound Analogue:0PX Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jldA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:0PP
2hpeA Unbound Unbound Unbound Bound:UNK-UNK-UNK-UNK-UNK-UNK-UNK-UNK-UNK Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hpfA Unbound Unbound Unbound Bound:UNK-UNK-UNK-UNK-UNK-UNK-UNK-UNK Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2mipA Unbound Unbound Unbound Analogue:PHE-VAL-PHE-LEU-GLU-ILE-NH2 (chain E,G) Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2mipC Unbound Unbound Unbound Analogue:PHE-VAL-PHE-LEU-GLU-ILE-NH2 (chain F,H) Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3upjA Unbound Unbound Unbound Analogue:U03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4upjA Unbound Unbound Unbound Analogue:U04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
5upjA Unbound Unbound Unbound Analogue:UIN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
6upjA Unbound Unbound Unbound Analogue:NIU Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hiiB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hshB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hshD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hsiB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1idaB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1idbB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ivpB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ivqB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jldB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hpeB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hpfB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2mipB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2mipD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3upjB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4upjB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
5upjB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
6upjB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2B01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2B02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2A03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2B03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2A04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2B04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mu2A05 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kA01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kB01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kE01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kF01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kI01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kJ01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kM01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kN01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kQ01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kR01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kU01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kV01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kY01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kZ01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kc01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kd01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kg01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kh01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kk01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kl01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9ko01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kp01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9ks01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kt01 Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aubA Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1e0eA Unbound Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kA02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kB02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kE02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kF02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kI02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kJ02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kM02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kN02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kQ02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kR02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kU02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kV02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kY02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kZ02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kc02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kd02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kg02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kh02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kk02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kl02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9ko02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kp02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9ks02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3f9kt02 Bound:_MG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1aub & literature [6], M00135, M00146

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1hiiA ASP 25 (EC 3.4.23.47)
1hshA ASP 25 (EC 3.4.23.47)
1hshC ASP 25 (EC 3.4.23.47)
1hsiA ASP 25 (EC 3.4.23.47)
1idaA ASP 25 (EC 3.4.23.47)
1idbA ASP 25 (EC 3.4.23.47)
1ivpA ASP 25 (EC 3.4.23.47) mutant K57L
1ivqA ASP 25 (EC 3.4.23.47) mutant K57L
1jldA ASP 25 (EC 3.4.23.47)
2hpeA ASP 25 (EC 3.4.23.47) mutant K57L
2hpfA ASP 25 (EC 3.4.23.47) mutant K57L
2mipA ASP 25 (EC 3.4.23.47)
2mipC ASP 25 (EC 3.4.23.47)
3upjA ASP 25 (EC 3.4.23.47) mutant K57L
4upjA ASP 25 (EC 3.4.23.47) mutant K57L
5upjA ASP 25 (EC 3.4.23.47) mutant K57L
6upjA ASP 25 (EC 3.4.23.47) mutant K57L
1hiiB ASP 25 (EC 3.4.23.47)
1hshB ASP 25 (EC 3.4.23.47)
1hshD ASP 25 (EC 3.4.23.47)
1hsiB ASP 25 (EC 3.4.23.47)
1idaB ASP 25 (EC 3.4.23.47)
1idbB ASP 25 (EC 3.4.23.47)
1ivpB ASP 25 (EC 3.4.23.47) mutant K57L
1ivqB ASP 25 (EC 3.4.23.47) mutant K57L
1jldB ASP 25 (EC 3.4.23.47)
2hpeB ASP 25 (EC 3.4.23.47) mutant K57L
2hpfB ASP 25 (EC 3.4.23.47) mutant K57L
2mipB ASP 25 (EC 3.4.23.47)
2mipD ASP 25 (EC 3.4.23.47)
3upjB ASP 25 (EC 3.4.23.47) mutant K57L
4upjB ASP 25 (EC 3.4.23.47) mutant K57L
5upjB ASP 25 (EC 3.4.23.47) mutant K57L
6upjB ASP 25 (EC 3.4.23.47) mutant K57L
1mu2A01
1mu2B01
1mu2A02 ASP 110;ASP 185;ASP 186(Magnesium binding) ASP 113;ALA 114 (EC 2.7.7.49 & 2.7.7.7)
1mu2B02
1mu2A03
1mu2B03
1mu2A04
1mu2B04
1mu2A05 ASP 442;ASP 497(Magnesium binding) (EC 3.1.26.4)
3f9kA01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kB01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kE01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kF01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kI01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kJ01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kM01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kN01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kQ01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kR01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kU01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kV01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kY01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kZ01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kc01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kd01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kg01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kh01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kk01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kl01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9ko01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kp01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9ks01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kt01 HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
1aubA HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
1e0eA HIS 12;HIS 16;CYS 40;CYS 43(Zinc binding) (integrase)
3f9kA02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kB02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kE02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kF02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kI02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kJ02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kM02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kN02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kQ02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kR02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kU02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kV02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kY02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kZ02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kc02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kd02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kg02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kh02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kk02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kl02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9ko02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kp02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9ks02 ASP 64;ASP 116(Magnesium binding) (integrase)
3f9kt02 ASP 64;ASP 116(Magnesium binding) (integrase)

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 1812757
Journal Adv Exp Med Biol
Year 1991
Volume 306
Pages 549-53
Authors Gustchina A, Weber IT, Wlodawer A
Title Molecular modeling of the HIV-2 protease.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2001747
Journal FEBS Lett
Year 1991
Volume 279
Pages 356-60
Authors Tozser J, Gustchina A, Weber IT, Blaha I, Wondrak EM, Oroszlan S
Title Studies on the role of the S4 substrate binding site of HIV proteinases.
Related PDB
Related UniProtKB
[3]
Resource
Comments Theoretical model
Medline ID
PubMed ID 1946342
Journal Proteins
Year 1991
Volume 10
Pages 325-39
Authors Gustchina A, Weber IT
Title Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases.
Related PDB 1phv 2phv
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8241159
Journal Biochemistry
Year 1993
Volume 32
Pages 13054-60
Authors Zhao B, Winborne E, Minnich MD, Culp JS, Debouck C, Abdel-Meguid SS
Title Three-dimensional structure of a simian immunodeficiency virus protease/inhibitor complex. Implications for the design of human immunodeficiency virus type 1 and 2 protease inhibitors.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8087563
Journal Bioorg Med Chem
Year 1993
Volume 1
Pages 415-22
Authors Sui Z, Salto R, Li J, Craik C, Ortiz de Montellano PR
Title Inhibition of the HIV-1 and HIV-2 proteases by curcumin and curcumin boron complexes.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8514751
Journal J Biol Chem
Year 1993
Volume 268
Pages 13103-9
Authors Mulichak AM, Hui JO, Tomasselli AG, Heinrikson RL, Curry KA, Tomich CS, Thaisrivongs S, Sawyer TK, Watenpaugh KD
Title The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-184.
Medline ID 93391360
PubMed ID 8378311
Journal Proc Natl Acad Sci U S A
Year 1993
Volume 90
Pages 8387-91
Authors Tong L, Pav S, Pargellis C, Do F, Lamarre D, Anderson PC
Title Crystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structures.
Related PDB 2mip
Related UniProtKB P04584
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-184 IN COMPLEX WITH INHIB.
Medline ID 95014470
PubMed ID 7929352
Journal J Biol Chem
Year 1994
Volume 269
Pages 26344-8
Authors Chen Z, Li Y, Chen E, Hall DL, Darke PL, Culberson C, Shafer JA, Kuo LC
Title Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases.
Related PDB 1hsh 1hsi
Related UniProtKB P04584
[9]
Resource
Comments
Medline ID
PubMed ID 8035428
Journal J Med Chem
Year 1994
Volume 37
Pages 2206-15
Authors Oprea TI, Waller CL, Marshall GR
Title Three-dimensional quantitative structure-activity relationship of human immunodeficiency virus (I) protease inhibitors. 2. Predictive power using limited exploration of alternate binding modes.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7526778
Journal Annu Rev Biochem
Year 1994
Volume 63
Pages 133-73
Authors Katz RA, Skalka AM
Title The retroviral enzymes.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7783120
Journal J Med Chem
Year 1995
Volume 38
Pages 1884-91
Authors Romines KR, Watenpaugh KD, Tomich PK, Howe WJ, Morris JK, Lovasz KD, Mulichak AM, Finzel BC, Lynn JC, Horng MM, et al
Title Use of medium-sized cycloalkyl rings to enhance secondary binding: discovery of a new class of human immunodeficiency virus (HIV) protease inhibitors.
Related PDB 5upj 6upj
Related UniProtKB
[12]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7658450
Journal J Med Chem
Year 1995
Volume 38
Pages 3624-37
Authors Thaisrivongs S, Watenpaugh KD, Howe WJ, Tomich PK, Dolak LA, Chong KT, Tomich CC, Tomasselli AG, Turner SR, Strohbach JW, et al
Title Structure-based design of novel HIV protease inhibitors: carboxamide-containing 4-hydroxycoumarins and 4-hydroxy-2-pyrones as potent nonpeptidic inhibitors.
Related PDB 3upj 4upj
Related UniProtKB
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-184 IN COMPLEX WITH INHIB.
Medline ID 95338600
PubMed ID 7613867
Journal Structure
Year 1995
Volume 3
Pages 381-9
Authors Priestle JP, Fassler A, Rosel J, Tintelnot-Blomley M, Strop P, Grutter MG
Title Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases in complex with CGP 53820, a novel pseudosymmetric inhibitor.
Related PDB 1hii
Related UniProtKB P04584
[14]
Resource
Comments
Medline ID
PubMed ID 7743130
Journal Structure
Year 1995
Volume 3
Pages 33-40
Authors Tong L, Pav S, Mui S, Lamarre D, Yoakim C, Beaulieu P, Anderson PC
Title Crystal structures of HIV-2 protease in complex with inhibitors containing the hydroxyethylamine dipeptide isostere.
Related PDB
Related UniProtKB
[15]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 86-184 IN COMPLEX WITH INHIB.
Medline ID 97359919
PubMed ID 9216835
Journal J Med Chem
Year 1997
Volume 40
Pages 2164-76
Authors Beaulieu PL, Wernic D, Abraham A, Anderson PC, Bogri T, Bousquet Y, Croteau G, Guse I, Lamarre D, Liard F, Paris W, Thibeault D, Pav S, Tong L
Title Potent HIV protease inhibitors containing a novel (hydroxyethyl)amide isostere.
Related PDB 1jld
Related UniProtKB P04584
[16]
Resource
Comments
Medline ID
PubMed ID 9209317
Journal Leukemia
Year 1997
Volume 11 Suppl 3
Pages 120-2
Authors Pichova I, Weber J, Litera J, Konvalinka J, Vondrasek J, Soucek M, Strop P, Majer P, Heuser AM, Kraeusslich HG
Title Peptide inhibitors of HIV-1 and HIV-2 proteases: a comparative study.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9368756
Journal Curr Biol
Year 1997
Volume 7
Pages 739-46
Authors Eijkelenboom AP, van den Ent FM, Vos A, Doreleijers JF, Hard K, Tullius TD, Plasterk RH, Kaptein R, Boelens R
Title The solution structure of the amino-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9692985
Journal Biochemistry
Year 1998
Volume 37
Pages 10928-36
Authors Swairjo MA, Towler EM, Debouck C, Abdel-Meguid SS
Title Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9557677
Journal J Virol
Year 1998
Volume 72
Pages 3916-24
Authors van den Ent FM, Vos A, Plasterk RH
Title Mutational scan of the human immunodeficiency virus type 2 integrase protein.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 10491141
Journal Eur J Biochem
Year 1999
Volume 264
Pages 921-9
Authors Boross P, Bagossi P, Copeland TD, Oroszlan S, Louis JM, Tozser J
Title Effect of substrate residues on the P2' preference of retroviral proteinases.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 10631984
Journal Protein Sci
Year 1999
Volume 8
Pages 2686-96
Authors Lescar J, Brynda J, Rezacova P, Stouracova R, Riottot MM, Chitarra V, Fabry M, Horejsi M, Sedlacek J, Bentley GA
Title Inhibition of the HIV-1 and HIV-2 proteases by a monoclonal antibody.
Related PDB
Related UniProtKB
[22]
Resource
Comments NMR structure
Medline ID
PubMed ID 11101216
Journal J Biomol NMR
Year 2000
Volume 18
Pages 119-28
Authors Eijkelenboom AP, van den Ent FM, Wechselberger R, Plasterk RH, Kaptein R, Boelens R
Title Refined solution structure of the dimeric N-terminal HHCC domain of HIV-2 integrase.
Related PDB 1aub
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11591344
Journal Structure (Camb)
Year 2001
Volume 9
Pages 887-95
Authors Rezacova P, Lescar J, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley GA
Title Structural basis of HIV-1 and HIV-2 protease inhibition by a monoclonal antibody.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 12386343
Journal Proc Natl Acad Sci U S A
Year 2002
Volume 99
Pages 14410-5
Authors Ren J, Bird LE, Chamberlain PP, Stewart-Jones GB, Stuart DI, Stammers DK
Title Structure of HIV-2 reverse transcriptase at 2.35-A resolution and the mechanism of resistance to non-nucleoside inhibitors.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 12511797
Journal J Synchrotron Radiat
Year 2003
Volume 10
Pages 86-95
Authors Feiters MC, Eijkelenboom AP, Nolting HF, Krebs B, van den Ent FM, Plasterk RH, Kaptein R, Boelens R
Title X-ray absorption spectroscopic studies of zinc in the N-terminal domain of HIV-2 integrase and model compounds.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 19132083
Journal PLoS Pathog
Year 2009
Volume 5
Pages e1000259
Authors Hare S, Shun MC, Gupta SS, Valkov E, Engelman A, Cherepanov P
Title A novel co-crystal structure affords the design of gain-of-function lentiviral integrase mutants in the presence of modified PSIP1/LEDGF/p75.
Related PDB 3f9k
Related UniProtKB

Comments
The protein, POL polyprotein (Swiss-prot; P04584) from HIV-2, is composed of the following enzymes, protease (E.C. 3.4.23.47), reverse transcriptase (E.C. 2.7.7.49 & 2.7.7.7), ribonuclease H (E.C. 3.1.26.4) and integrase.
This entry corresponds to the protease domain (residues 86-184), and the reverse transcriptase and ribonuclease H (residues 613-1171) and a non-catalytic region of integrase (residues 1224-1464) of this protein (Swiss-prot;P04584).
###
The protease domain form a homodimer to function as an enzyme. This enzyme domain belongs to the peptidase family-A2.
The homodimer of this domain contains a catalytic dyad, composed of two aspartic acid residues, suggesting that it has a similar catalytic mechanism to that of pepsin (D00436 in EzCatDB).
###
According to the literature [17], the C-terminal structure (PDB;1e0e) corresponds to the N-terminal domain of integrase, which catalyzes cleavage of viral DNA, and integration of the cleaved DNA into the target DNA. However, the catalytic domain of this enzyme has not been determined yet.
The paper [10] mentioned that zinc binding in this domain stabilizes its structure, instead of contributing to the catalysis.
###
On the other hand, the N-terminal domains of 1mu2 (PDB) correspond to reverse transcriptase (E.C. 2.7.7.49), whilst the fifth domain of 1mu2 corresponds to ribonuclease H (E.C. 3.1.26.4). Considering the structural similarity to that of M00146, the ribonuclease H must have got a binding site for magnesium or manganese ion at the catalytic site.
Since the catalytic site of the reverse transcriptase (E.C. 2.7.7.49) is homologous to that of its homologous enzyme from Moloney murine leukemia virus (M00135 in EzCatDB), its catalytic mechanism must be similar to that of the homologous enzyme.

Created Updated
2002-09-10 2012-06-29