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Magnesium in PDB 3ck4: A Heterospecific Leucine Zipper Tetramer

Protein crystallography data

The structure of A Heterospecific Leucine Zipper Tetramer, PDB code: 3ck4 was solved by J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.18 / 1.70
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 48.846, 49.107, 51.917, 115.77, 94.21, 109.62
R / Rfree (%) 17.1 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the A Heterospecific Leucine Zipper Tetramer (pdb code 3ck4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the A Heterospecific Leucine Zipper Tetramer, PDB code: 3ck4:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 3ck4

Go back to Magnesium Binding Sites List in 3ck4
Magnesium binding site 1 out of 4 in the A Heterospecific Leucine Zipper Tetramer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of A Heterospecific Leucine Zipper Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg35

b:21.9
occ:1.00
O C:HOH66 2.0 32.7 1.0
NE2 C:HIS19 2.2 15.9 1.0
O B:HOH42 2.3 26.6 1.0
O B:HOH39 2.4 25.6 1.0
NE2 B:HIS19 2.5 21.1 1.0
CD2 C:HIS19 3.2 14.1 1.0
CE1 C:HIS19 3.2 19.2 1.0
CD2 B:HIS19 3.4 19.8 1.0
CE1 B:HIS19 3.5 22.3 1.0
ND1 C:HIS19 4.4 13.7 1.0
CG C:HIS19 4.4 14.4 1.0
ND1 B:HIS19 4.6 21.9 1.0
CG B:HIS19 4.6 18.7 1.0
CB B:SER15 4.6 15.0 1.0
CB C:SER15 4.6 20.2 1.0
OG B:SER15 4.7 17.8 1.0
OG C:SER15 5.0 25.1 1.0

Magnesium binding site 2 out of 4 in 3ck4

Go back to Magnesium Binding Sites List in 3ck4
Magnesium binding site 2 out of 4 in the A Heterospecific Leucine Zipper Tetramer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of A Heterospecific Leucine Zipper Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg35

b:22.6
occ:1.00
NE2 G:HIS19 2.4 18.5 1.0
NE2 F:HIS19 2.4 18.2 1.0
O G:HOH51 2.6 32.9 1.0
CD2 G:HIS19 3.3 16.5 1.0
CE1 F:HIS19 3.3 21.2 1.0
CE1 G:HIS19 3.4 22.7 1.0
CD2 F:HIS19 3.4 15.8 1.0
ND1 F:HIS19 4.5 16.4 1.0
ND1 G:HIS19 4.5 18.1 1.0
O F:HOH58 4.5 32.6 1.0
CG G:HIS19 4.5 16.7 1.0
CG F:HIS19 4.5 14.2 1.0
CB G:SER15 4.6 15.6 1.0
OG G:SER15 4.7 19.6 1.0
CB F:SER15 4.9 17.0 1.0

Magnesium binding site 3 out of 4 in 3ck4

Go back to Magnesium Binding Sites List in 3ck4
Magnesium binding site 3 out of 4 in the A Heterospecific Leucine Zipper Tetramer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of A Heterospecific Leucine Zipper Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg35

b:33.2
occ:1.00
O I:HOH146 1.9 26.6 1.0
O I:HOH176 2.1 29.9 1.0
OD2 I:ASP8 4.1 28.7 1.0
OD1 I:ASP8 4.2 26.6 1.0
O I:HOH56 4.2 26.6 1.0
CG I:ASP8 4.6 26.3 1.0
CD I:LYS4 4.6 41.8 1.0
O I:HOH94 5.0 36.4 1.0

Magnesium binding site 4 out of 4 in 3ck4

Go back to Magnesium Binding Sites List in 3ck4
Magnesium binding site 4 out of 4 in the A Heterospecific Leucine Zipper Tetramer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of A Heterospecific Leucine Zipper Tetramer within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg35

b:13.7
occ:1.00
O J:HOH41 2.1 13.5 1.0
O K:HOH88 2.1 17.9 1.0
O K:HOH85 2.1 15.8 1.0
O J:HOH73 2.2 17.5 1.0
NE2 K:HIS19 2.2 15.4 1.0
NE2 J:HIS19 2.3 14.1 1.0
CE1 K:HIS19 3.1 18.2 1.0
CE1 J:HIS19 3.2 17.1 1.0
CD2 K:HIS19 3.3 13.4 1.0
CD2 J:HIS19 3.3 12.5 1.0
O J:HOH40 4.1 21.3 1.0
O J:HOH52 4.2 25.2 1.0
O K:HOH61 4.2 18.4 1.0
ND1 K:HIS19 4.3 13.1 1.0
ND1 J:HIS19 4.3 15.1 1.0
CG K:HIS19 4.4 13.0 1.0
CG J:HIS19 4.4 14.7 1.0

Reference:

Y.Deng, J.Liu, Q.Zheng, Q.Li, N.R.Kallenbach, M.Lu. A Heterospecific Leucine Zipper Tetramer. Chem.Biol. V. 15 908 2008.
ISSN: ISSN 1074-5521
PubMed: 18804028
DOI: 10.1016/J.CHEMBIOL.2008.07.008
Page generated: Wed Aug 14 11:25:02 2024

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