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Magnesium in PDB 2w00: Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp

Enzymatic activity of Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp

All present enzymatic activity of Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp:
3.1.21.3;

Protein crystallography data

The structure of Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp, PDB code: 2w00 was solved by M.Lapkouski, S.Panjikar, I.Kuta Smatanova, R.Ettrich, E.Csefalvay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.97 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 123.910, 129.922, 161.010, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 26.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp (pdb code 2w00). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp, PDB code: 2w00:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2w00

Go back to Magnesium Binding Sites List in 2w00
Magnesium binding site 1 out of 2 in the Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1887

b:11.7
occ:1.00
O3G A:ATP1886 1.9 24.8 1.0
OG1 A:THR314 2.0 43.6 1.0
O A:HOH2280 2.0 20.7 1.0
O A:HOH2283 2.1 23.8 1.0
O1B A:ATP1886 2.1 17.8 1.0
PG A:ATP1886 3.2 29.7 1.0
CB A:THR314 3.3 43.3 1.0
PB A:ATP1886 3.4 26.8 1.0
O3B A:ATP1886 3.6 31.1 1.0
OD2 A:ASP408 4.0 45.1 1.0
O A:HOH2149 4.1 18.8 1.0
CG2 A:THR314 4.1 43.9 1.0
O1A A:ATP1886 4.1 26.9 1.0
O1G A:ATP1886 4.2 33.7 1.0
N A:THR314 4.2 43.5 1.0
O A:GLY662 4.2 39.0 1.0
O2G A:ATP1886 4.2 30.2 1.0
CA A:THR314 4.3 43.5 1.0
OD1 A:ASP408 4.3 39.7 1.0
O3A A:ATP1886 4.4 27.7 1.0
NZ A:LYS313 4.5 32.6 1.0
CA A:GLY662 4.5 37.8 1.0
O2B A:ATP1886 4.5 24.2 1.0
PA A:ATP1886 4.6 25.3 1.0
CG A:ASP408 4.6 39.6 1.0
O2A A:ATP1886 4.7 25.4 1.0
O A:HOH2123 4.8 29.9 1.0
C A:GLY662 4.9 39.4 1.0
O A:HOH2127 4.9 27.6 1.0

Magnesium binding site 2 out of 2 in 2w00

Go back to Magnesium Binding Sites List in 2w00
Magnesium binding site 2 out of 2 in the Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1894

b:13.3
occ:1.00
O3G B:ATP1893 1.9 22.6 1.0
O B:HOH2103 1.9 28.4 1.0
O B:HOH2293 2.0 22.9 1.0
OG1 B:THR314 2.0 43.6 1.0
O B:HOH2133 2.1 25.6 1.0
O1B B:ATP1893 2.1 28.8 1.0
PG B:ATP1893 3.3 23.7 1.0
PB B:ATP1893 3.3 26.7 1.0
CB B:THR314 3.3 44.2 1.0
O3B B:ATP1893 3.6 25.9 1.0
OD2 B:ASP408 3.8 42.7 1.0
N B:THR314 4.0 43.2 1.0
O B:HOH2134 4.0 34.9 1.0
O1G B:ATP1893 4.0 21.0 1.0
OD1 B:ASP408 4.1 39.4 1.0
CA B:THR314 4.2 43.9 1.0
NZ B:LYS313 4.3 32.9 1.0
O2B B:ATP1893 4.3 28.7 1.0
CG2 B:THR314 4.3 43.9 1.0
O1A B:ATP1893 4.3 29.8 1.0
O2G B:ATP1893 4.4 20.3 1.0
CG B:ASP408 4.4 39.6 1.0
O3A B:ATP1893 4.4 33.3 1.0
O B:GLY662 4.5 39.1 1.0
PA B:ATP1893 4.7 29.5 1.0
CA B:GLY662 4.7 38.2 1.0
CB B:LYS313 4.7 42.0 1.0
O B:HOH2114 4.8 24.5 1.0
O2A B:ATP1893 4.8 28.8 1.0
C B:LYS313 4.9 46.0 1.0

Reference:

M.Lapkouski, S.Panjikar, P.Janscak, I.K.Smatanova, J.Carey, R.Ettrich, E.Csefalvay. Structure of the Motor Subunit of Type I Restriction-Modification Complex ECOR124I. Nat.Struct.Mol.Biol. V. 16 94 2009.
ISSN: ISSN 1545-9993
PubMed: 19079266
DOI: 10.1038/NSMB.1523
Page generated: Mon Dec 14 07:43:23 2020

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