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Magnesium in PDB 4zck: Crystal Structure of C-Terminal Fragment of Escherichia Coli Bipa/Typa

Protein crystallography data

The structure of Crystal Structure of C-Terminal Fragment of Escherichia Coli Bipa/Typa, PDB code: 4zck was solved by H.T.Fan, J.Hahm, S.Diggs, G.Blaha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.00 / 2.48
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 83.562, 83.562, 191.841, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of C-Terminal Fragment of Escherichia Coli Bipa/Typa (pdb code 4zck). 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 C-Terminal Fragment of Escherichia Coli Bipa/Typa, PDB code: 4zck:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4zck

Go back to Magnesium Binding Sites List in 4zck
Magnesium binding site 1 out of 2 in the Crystal Structure of C-Terminal Fragment of Escherichia Coli Bipa/Typa


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 C-Terminal Fragment of Escherichia Coli Bipa/Typa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:0.5
occ:1.00
O A:ASN485 3.2 95.9 1.0
OD2 A:ASP573 3.4 0.9 1.0
O A:ARG483 3.8 90.6 1.0
O A:GLN484 3.9 98.7 1.0
C A:ASN485 4.2 92.2 1.0
O A:SER530 4.2 95.2 1.0
C A:GLN484 4.3 90.8 1.0
NH2 A:ARG483 4.3 68.2 1.0
CD A:ARG483 4.5 79.1 1.0
CG A:ASP573 4.5 0.4 1.0
C A:ARG483 4.6 87.2 1.0
N A:ASN485 4.8 86.5 1.0
CA A:GLN484 4.9 89.6 1.0
OD1 A:ASP573 5.0 0.2 1.0

Magnesium binding site 2 out of 2 in 4zck

Go back to Magnesium Binding Sites List in 4zck
Magnesium binding site 2 out of 2 in the Crystal Structure of C-Terminal Fragment of Escherichia Coli Bipa/Typa


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 C-Terminal Fragment of Escherichia Coli Bipa/Typa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:0.3
occ:1.00
O A:HOH1121 2.2 83.7 1.0
O A:HOH1130 2.4 99.8 1.0
O A:GLU570 2.4 76.8 1.0
O A:GLY481 2.6 79.0 1.0
O A:HOH1116 2.7 75.4 1.0
O A:HOH1120 2.8 73.2 1.0
C A:GLU570 3.5 69.6 1.0
O A:ILE572 3.5 71.3 1.0
C A:GLY481 3.7 78.5 1.0
CA A:GLN482 4.2 84.4 1.0
CA A:GLU570 4.2 75.3 1.0
O A:LEU569 4.2 69.3 1.0
N A:GLN482 4.4 81.0 1.0
C A:PHE571 4.4 67.4 1.0
O A:PHE571 4.4 78.0 1.0
N A:PHE571 4.4 59.0 1.0
O A:HOH1131 4.5 76.7 1.0
N A:ARG483 4.5 83.8 1.0
C A:ILE572 4.6 73.4 1.0
N A:ILE572 4.7 66.9 1.0
CD A:ARG384 4.7 71.2 1.0
CA A:PHE571 4.8 60.2 1.0
CA A:GLY481 4.8 79.1 1.0
NH1 A:ARG384 4.9 76.2 1.0
C A:GLN482 4.9 83.5 1.0
CG A:GLN482 4.9 0.5 1.0

Reference:

H.Fan, J.Hahm, S.Diggs, J.J.Perry, G.Blaha. Structural and Functional Analysis of Bipa, A Regulator of Virulence in Enteropathogenic Escherichia Coli. J.Biol.Chem. V. 290 20856 2015.
ISSN: ESSN 1083-351X
PubMed: 26163516
DOI: 10.1074/JBC.M115.659136
Page generated: Sat Sep 28 23:57:50 2024

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