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Magnesium in PDB 3zlm: Fic Protein From Neisseria Meningitidis Mutant E186G in Complex with Amppnp

Protein crystallography data

The structure of Fic Protein From Neisseria Meningitidis Mutant E186G in Complex with Amppnp, PDB code: 3zlm was solved by A.Goepfert, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 149.080, 149.080, 76.440, 90.00, 90.00, 120.00
R / Rfree (%) 17.81 / 19.588

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Fic Protein From Neisseria Meningitidis Mutant E186G in Complex with Amppnp (pdb code 3zlm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Fic Protein From Neisseria Meningitidis Mutant E186G in Complex with Amppnp, PDB code: 3zlm:

Magnesium binding site 1 out of 1 in 3zlm

Go back to Magnesium Binding Sites List in 3zlm
Magnesium binding site 1 out of 1 in the Fic Protein From Neisseria Meningitidis Mutant E186G in Complex with Amppnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fic Protein From Neisseria Meningitidis Mutant E186G in Complex with Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:64.8
occ:0.80
O2B A:ANP300 2.3 51.2 0.8
O1A A:ANP300 2.5 46.1 0.8
PB A:ANP300 3.4 50.7 0.8
PA A:ANP300 3.5 47.4 0.8
N3B A:ANP300 3.8 55.4 0.8
O3A A:ANP300 3.9 48.6 0.8
OE1 A:GLU111 3.9 65.7 1.0
O2A A:ANP300 4.1 43.2 0.8
N A:GLY112 4.2 42.3 1.0
NH2 A:ARG115 4.3 45.7 1.0
CB A:GLU111 4.4 47.8 1.0
CA A:GLU111 4.7 45.5 1.0
CG A:GLU111 4.8 53.8 1.0
O1B A:ANP300 4.8 48.0 0.8
CD A:GLU111 4.8 61.0 1.0
O5' A:ANP300 4.9 48.3 0.8
O A:HOH2085 5.0 47.2 1.0

Reference:

A.Goepfert, F.V.Stanger, C.Dehio, T.Schirmer. Conserved Inhibitory Mechanism and Competent Atp Binding Mode For Adenylyltransferases with Fic Fold. Plos One V. 8 64901 2013.
ISSN: ISSN 1932-6203
PubMed: 23738009
DOI: 10.1371/JOURNAL.PONE.0064901
Page generated: Mon Dec 14 09:03:57 2020

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