Brand  (β version)

PDB ID: 1CZB

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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 : 1CZB   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN FROM HEPES
Release Data : 1999-09-08
Compound :
mol_id molecule chains
1 AVIAN SARCOMA VIRUS INTEGRASE A
fragment: CATALYTIC CORE DOMAIN
mutation: INS(P48, L49, R50, E51, N208, L209)
Source :
mol_id organism_scientific expression_system
1 Avian sarcoma virus  (taxid:11876) Escherichia coli  (taxid:562)
expression_system_plasmid: PRC23IN(52-207)
Authors : Lubkowski, J., Dauter, Z., Yang, F., Alexandratos, J., Merkel, G., Skalka, A.M., Wlodawer, A.
Keywords : MIXED BETA-SHEET SURROUNDED BY ALPHA-HELICES, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.06 Å )
Citation :

Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant.

Lubkowski, J.,Dauter, Z.,Yang, F.  et al.
(1999)  Biochemistry  38 : 13512 - 13522

PubMed: 10521258
DOI: 10.1021/bi991362q

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.