Brand  (β version)

PDB ID: 1A5V

Hetero Atom Contents

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Code Name Style Show Link
MN Manganese (II) ion PoSSuM
Y3 4-acetylamino-5-hydroxynaphthalene-2,7-disulfonic acid PoSSuM

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Structure summary

Code : 1A5V   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3 AND MN CATION
Release Data : 1998-05-27
Compound :
mol_id molecule chains
1 INTEGRASE A
ec: 2.7.7.49
fragment: CATALYTIC CORE DOMAIN
other_details: P03354 FRAGMENT OF POLYPROTEIN POL-RSVP
Source :
mol_id organism_scientific expression_system
1 Rous sarcoma virus (strain Schmidt-Ruppin)  (taxid:11889) Escherichia coli  (taxid:562)
strain: Schmidt-Ruppin
expression_system_plasmid: PRC23IN(52-207)
other_details: SEE JRNL REFERENCE
Authors : Lubkowski, J., Yang, F., Alexandratos, J., Wlodawer, A.
Keywords : HYDROLASE, ENDONUCLEASE, HIV-1 INTEGRASE INHIBITOR
Exp. method : X-RAY DIFFRACTION ( 1.9 Å )
Citation :

Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor.

Lubkowski, J.,Yang, F.,Alexandratos, J.  et al.
(1998)  Proc.Natl.Acad.Sci.USA  95 : 4831 - 4836

PubMed: 9560188
DOI: 10.1073/pnas.95.9.4831

Reaction

Chain : A
UniProt : P03354 (POL_RSVP)
Reaction: EC: Evidence:
Physiological Direction:
[Reverse transcriptase alpha-subunit]
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 		2.7.7.49 PROSITE-ProRule:PRU00405
-
[Reverse transcriptase alpha-subunit]
DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate 		2.7.7.7 PROSITE-ProRule:PRU00405
-
[Reverse transcriptase alpha-subunit]
Endonucleolytic cleavage to 5'-phosphomonoester. 		3.1.26.4 PROSITE-ProRule:PRU00408
-
Cofactor: Evidence: Note:
Mg(2+) ECO:0000250
The RT polymerase active site binds 2 magnesium ions.
Mg(2+) ECO:0000250
Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.
Mn(2+) ECO:0000269 | PubMed:11024025
ECO:0000269 | PubMed:11024025
Binds 8 Mg(2+) ions per integrase homotetramer. Zn(2+) can also be a cofactor for the nicking activity, but not for the polynucleotidyltransferase activity.