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Calcium in PDB 3k9j: Transposase Domain of Metnase

Enzymatic activity of Transposase Domain of Metnase

All present enzymatic activity of Transposase Domain of Metnase:
2.1.1.43;

Protein crystallography data

The structure of Transposase Domain of Metnase, PDB code: 3k9j was solved by K.D.Goodwin, H.He, T.Imasaki, S.-H.Lee, M.M.Georgiadis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.59 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 79.158, 45.411, 90.678, 90.00, 113.81, 90.00
R / Rfree (%) 20.5 / 23.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Transposase Domain of Metnase (pdb code 3k9j). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Transposase Domain of Metnase, PDB code: 3k9j:

Calcium binding site 1 out of 1 in 3k9j

Go back to Calcium Binding Sites List in 3k9j
Calcium binding site 1 out of 1 in the Transposase Domain of Metnase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Transposase Domain of Metnase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1

b:64.1
occ:1.00
O A:HOH148 2.6 53.6 1.0
O A:HOH144 2.7 49.4 1.0
OD1 A:ASP483 2.8 45.5 1.0
O A:HOH240 2.8 57.1 1.0
OD2 A:ASP483 2.9 51.6 1.0
CG A:ASP483 3.2 41.5 1.0
O A:HOH241 3.5 56.8 1.0
OD1 A:ASP575 3.9 48.4 1.0
O A:HOH269 4.1 61.3 1.0
OD1 A:ASN610 4.2 47.9 1.0
CG A:ASP575 4.2 51.0 1.0
ND2 A:ASN610 4.2 44.7 1.0
O A:HOH267 4.5 59.2 1.0
O A:HOH268 4.5 57.0 1.0
O A:HOH146 4.6 51.7 1.0
OD2 A:ASP575 4.6 50.7 1.0
CG A:ASN610 4.6 46.5 1.0
O A:HOH64 4.7 40.3 1.0
O A:GLU484 4.7 37.4 1.0
CB A:ASP483 4.7 32.5 1.0
CB A:ASP575 4.8 41.6 1.0

Reference:

K.D.Goodwin, H.He, T.Imasaki, S.H.Lee, M.M.Georgiadis. Crystal Structure of the Human HSMAR1-Derived Transposase Domain in the Dna Repair Enzyme Metnase. Biochemistry V. 49 5705 2010.
ISSN: ISSN 0006-2960
PubMed: 20521842
DOI: 10.1021/BI100171X
Page generated: Sat Dec 12 04:17:21 2020

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