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Magnesium in PDB 4beb: Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp

Enzymatic activity of Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp

All present enzymatic activity of Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp:
3.1.21.3;

Protein crystallography data

The structure of Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp, PDB code: 4beb was solved by E.Csefalvay, M.Lapkouski, A.Guzanova, L.Csefalvay, T.Baikova, I.Shevelev, P.Janscak, I.K.Smatanova, S.Panjikar, J.Carey, M.Weiserova, R.Ettrich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.885 / 2.99
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 127.112, 123.112, 160.110, 90.00, 111.48, 90.00
R / Rfree (%) 25.5 / 29.65

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp (pdb code 4beb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp, PDB code: 4beb:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4beb

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Magnesium binding site 1 out of 4 in the Mutant (K220E) 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 Mutant (K220E) 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:Mg1885

b:45.2
occ:1.00
 O1B A:ATP1886 2.3 41.1 1.0
OG1 A:THR314 2.6 41.4 1.0
O3G A:ATP1886 3.0 39.9 1.0
OD1 A:ASP408 3.3 30.6 1.0
PB A:ATP1886 3.3 44.5 1.0
OD2 A:ASP408 3.4 36.8 1.0
O3B A:ATP1886 3.4 51.7 1.0
N A:THR314 3.7 37.4 1.0
CG A:ASP408 3.7 32.6 1.0
PG A:ATP1886 3.8 34.1 1.0
CB A:THR314 3.8 42.5 1.0
CB A:LYS313 3.9 34.3 1.0
CA A:THR314 4.1 41.0 1.0
O2B A:ATP1886 4.2 29.3 1.0
O2G A:ATP1886 4.3 31.9 1.0
C A:LYS313 4.4 36.1 1.0
NZ A:LYS313 4.5 29.9 1.0
CB A:GLU409 4.5 48.1 1.0
O3A A:ATP1886 4.6 43.1 1.0
CA A:LYS313 4.6 37.2 1.0
CE A:LYS313 4.7 31.8 1.0
O1A A:ATP1886 4.8 35.2 1.0
CG2 A:THR314 5.0 43.1 1.0
N A:LYS313 5.0 44.5 1.0
OD2 A:ASP341 5.0 66.9 1.0

Magnesium binding site 2 out of 4 in 4beb

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Magnesium binding site 2 out of 4 in the Mutant (K220E) 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 Mutant (K220E) 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:Mg1885

b:52.2
occ:1.00
 O1B B:ATP1886 2.7 48.9 1.0
O2G B:ATP1886 3.2 57.4 1.0
OG1 B:THR314 3.2 45.7 1.0
OD1 B:ASP408 3.2 52.0 1.0
O3B B:ATP1886 3.4 58.4 1.0
PB B:ATP1886 3.5 55.6 1.0
O3G B:ATP1886 3.6 61.9 1.0
PG B:ATP1886 3.6 47.7 1.0
CB B:GLU409 3.8 62.4 1.0
CB B:LYS313 3.9 52.5 1.0
OD2 B:ASP408 3.9 55.5 1.0
CG B:ASP408 4.0 56.6 1.0
NZ B:LYS313 4.1 59.0 1.0
N B:THR314 4.1 53.7 1.0
O2B B:ATP1886 4.2 52.3 1.0
CE B:LYS313 4.3 57.8 1.0
CG B:GLU409 4.4 63.4 1.0
CB B:THR314 4.4 54.2 1.0
OD2 B:ASP341 4.5 76.6 1.0
CA B:THR314 4.6 54.6 1.0
C B:LYS313 4.6 52.8 1.0
CD B:LYS313 4.7 54.8 1.0
CA B:LYS313 4.8 54.6 1.0
O3A B:ATP1886 4.9 54.4 1.0
CG B:LYS313 4.9 52.3 1.0

Magnesium binding site 3 out of 4 in 4beb

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Magnesium binding site 3 out of 4 in the Mutant (K220E) 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 3 of Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1885

b:37.9
occ:1.00
 OG1 C:THR314 2.4 39.6 1.0
O1B C:ATP1886 2.6 34.1 1.0
OD1 C:ASP408 2.8 31.1 1.0
OD2 C:ASP408 3.1 40.6 1.0
O3G C:ATP1886 3.3 27.2 1.0
CG C:ASP408 3.4 35.5 1.0
N C:THR314 3.5 34.9 1.0
CB C:THR314 3.6 41.4 1.0
CA C:THR314 3.8 36.1 1.0
CB C:LYS313 3.9 32.8 1.0
PB C:ATP1886 4.0 39.1 1.0
C C:LYS313 4.2 34.2 1.0
CB C:GLU409 4.3 40.4 1.0
O3B C:ATP1886 4.4 40.3 1.0
PG C:ATP1886 4.5 28.8 1.0
CA C:LYS313 4.6 35.2 1.0
NZ C:LYS313 4.6 29.6 1.0
CG2 C:THR314 4.7 49.6 1.0
O1A C:ATP1886 4.8 33.4 1.0
CE C:LYS313 4.8 33.1 1.0
O2B C:ATP1886 4.9 26.7 1.0
CB C:ASP408 4.9 33.7 1.0
O C:LYS313 4.9 33.4 1.0
CD C:LYS313 5.0 31.4 1.0

Magnesium binding site 4 out of 4 in 4beb

Go back to Magnesium Binding Sites List in 4beb
Magnesium binding site 4 out of 4 in the Mutant (K220E) 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 4 of Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1885

b:67.8
occ:1.00
 O3G D:ATP1886 2.8 52.8 1.0
OD1 D:ASP408 3.0 55.7 1.0
O1B D:ATP1886 3.1 57.9 1.0
CB D:GLU409 3.3 60.3 1.0
O2G D:ATP1886 3.6 59.8 1.0
OG1 D:THR314 3.7 65.8 1.0
PG D:ATP1886 3.7 55.7 1.0
OD2 D:ASP408 3.8 55.7 1.0
CG D:ASP408 3.8 57.6 1.0
CG D:GLU409 3.9 71.9 1.0
PB D:ATP1886 3.9 55.4 1.0
NZ D:LYS313 4.1 61.1 1.0
CB D:LYS313 4.1 57.6 1.0
O3B D:ATP1886 4.1 62.6 1.0
OD2 D:ASP341 4.3 81.5 1.0
O2B D:ATP1886 4.4 55.5 1.0
CE D:LYS313 4.5 54.9 1.0
N D:THR314 4.6 59.0 1.0
CA D:GLU409 4.6 60.1 1.0
OE2 D:GLU409 4.7 71.3 1.0
N D:GLU409 4.7 61.4 1.0
CD D:GLU409 4.7 72.6 1.0
CD D:LYS313 4.8 49.6 1.0
C D:ASP408 4.9 61.4 1.0
CB D:THR314 4.9 64.2 1.0
C D:LYS313 5.0 57.4 1.0

Reference:

E.Csefalvay, M.Lapkouski, A.Guzanova, L.Csefalvay, T.Baikova, I.Shevelev, P.Janscak, I.K.Smatanova, S.Panjikar, J.Carey, M.Weiserova, R.Ettrich. Mutant (K220E) of the Hsdr Subunit of the ECOR124I Restriction Enzyme in Complex with Atp To Be Published.
Page generated: Thu Aug 15 16:26:58 2024

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