Brand  (β version)

PDB ID: 6CW4

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Ligands
Code Name Style Show Link
FGV (1r,2s,3r,4r,5s,6s)-2,4,6-trihydroxycyclohexane-1,3,5-triyl tris[dihydrogen (phosphate)] PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 6CW4   PDBj   RCSB PDB   PDBe
Header : VIRAL PROTEIN
Title : HADDOCK structure of the Rous sarcoma virus matrix protein (M-domain) in complex with inositol 1,3,5-trisphosphate
Release Data : 2018-10-24
Compound :
mol_id molecule chains
1 Matrix protein p19 A
fragment: residues 1-87
mutation: M1S
Source :
mol_id organism_scientific organism_common expression_system
1 Rous sarcoma virus  (taxid:11888) RSV-PrC Escherichia coli  (taxid:562)
strain: Prague C
gene: gag-pol
Authors : Vlach, J., Saad, J.S.
Keywords : RSV, ASV, Gag, I(1, 3, 5)P3, VIRAL PROTEIN
Exp. method : SOLUTION NMR
Citation :

Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly.

Vlach, J.,Eastep, G.N.,Ghanam, R.H.  et al.
(2018)  J. Biol. Chem.  293 : 18828 - 18840

PubMed: 30309983
DOI: 10.1074/jbc.RA118.003944

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.