Brand  (β version)

PDB ID: 1ASU

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Ligands
Code Name Style Show Link
EPE 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1ASU   PDBj   RCSB PDB   PDBe
Header : DNA INTEGRATION
Title : AVIAN SARCOMA VIRUS INTEGRASE CATALYTIC CORE DOMAIN CRYSTALLIZED FROM 2% PEG 400, 2M AMMONIUM SULFATE, HEPES PH 7.5
Release Data : 1995-11-14
Compound :
mol_id molecule chains
1 AVIAN SARCOMA VIRUS INTEGRASE A
mutation: INS(PRO 48, LEU 49, ARG 50, GLU 51, ASN 208, LEU 209)
other_details: CRYSTALLIZED FROM 2% PEG 400, 2M AMMONIUM SULFATE, HEPES PH 7.5
Source :
mol_id organism_scientific expression_system
1 Avian sarcoma virus  (taxid:11876) Escherichia coli  (taxid:562)
strain: SCHMIDT-RUPPIN B
expression_system_plasmid: PRC23IN(52-207)
Authors : Bujacz, G., Jaskolski, M., Alexandratos, J., Wlodawer, A.
Keywords : DNA INTEGRATION
Exp. method : X-RAY DIFFRACTION ( 1.70 Å )
Citation :

High-resolution structure of the catalytic domain of avian sarcoma virus integrase.

Bujacz, G.,Jaskolski, M.,Alexandratos, J.  et al.
(1995)  J.Mol.Biol.  253 : 333 - 346

PubMed: 7563093
DOI: 10.1006/jmbi.1995.0556

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.