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Manganese in PDB 2vhg: Crystal Structure of the ISHP608 Transposase in Complex with Right End 31-Mer Dna

Protein crystallography data

The structure of Crystal Structure of the ISHP608 Transposase in Complex with Right End 31-Mer Dna, PDB code: 2vhg was solved by O.Barabas, D.R.Ronning, C.Guynet, A.B.Hickman, B.Ton-Hoang, M.Chandler, F.Dyda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.0 / 2.9
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.466, 90.925, 93.418, 90.00, 90.00, 90.00
R / Rfree (%) 28.47 / 31.97

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the ISHP608 Transposase in Complex with Right End 31-Mer Dna (pdb code 2vhg). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the ISHP608 Transposase in Complex with Right End 31-Mer Dna, PDB code: 2vhg:

Manganese binding site 1 out of 1 in 2vhg

Go back to Manganese Binding Sites List in 2vhg
Manganese binding site 1 out of 1 in the Crystal Structure of the ISHP608 Transposase in Complex with Right End 31-Mer Dna


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the ISHP608 Transposase in Complex with Right End 31-Mer Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1132

b:97.2
occ:1.00
NE2 A:HIS64 2.6 82.4 1.0
OD2 A:ASP61 2.9 0.4 1.0
CE1 A:HIS64 3.1 82.5 1.0
ND1 A:HIS66 3.4 76.7 1.0
CD2 A:HIS64 3.8 82.1 1.0
CE1 A:HIS66 4.0 77.0 1.0
CG A:ASP61 4.1 0.2 1.0
ND1 A:HIS64 4.3 82.5 1.0
OE1 A:GLN59 4.4 0.6 1.0
CG A:HIS66 4.6 75.8 1.0
CG A:HIS64 4.7 81.8 1.0
OD1 A:ASP61 4.9 0.0 1.0

Reference:

O.Barabas, D.R.Ronning, C.Guynet, A.B.Hickman, B.Ton-Hoang, M.Chandler, F.Dyda. Mechanism of IS200/IS605 Family Dna Transposases: Activation and Transposon-Directed Target Site Selection. Cell(Cambridge,Mass.) V. 132 208 2008.
ISSN: ISSN 0092-8674
PubMed: 18243097
DOI: 10.1016/J.CELL.2007.12.029
Page generated: Tue Dec 15 04:05:50 2020

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