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Magnesium in PDB 7q6d: E. Coli Ftsa 1-405 Atp 3 Ni

Protein crystallography data

The structure of E. Coli Ftsa 1-405 Atp 3 Ni, PDB code: 7q6d was solved by T.Nierhaus, D.Kureisaite-Ciziene, J.Lowe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.64 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.102, 64.177, 65.285, 90, 96.07, 90
R / Rfree (%) 21.7 / 26.9

Other elements in 7q6d:

The structure of E. Coli Ftsa 1-405 Atp 3 Ni also contains other interesting chemical elements:

Nickel (Ni) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Ftsa 1-405 Atp 3 Ni (pdb code 7q6d). 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 E. Coli Ftsa 1-405 Atp 3 Ni, PDB code: 7q6d:

Magnesium binding site 1 out of 1 in 7q6d

Go back to Magnesium Binding Sites List in 7q6d
Magnesium binding site 1 out of 1 in the E. Coli Ftsa 1-405 Atp 3 Ni


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Ftsa 1-405 Atp 3 Ni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:24.6
occ:1.00
O1B A:ATP505 2.4 52.8 1.0
O3G A:ATP505 2.4 59.5 1.0
OE2 A:GLU14 2.4 37.6 1.0
CD A:GLU14 3.3 45.9 1.0
PB A:ATP505 3.5 37.9 1.0
OE1 A:GLU14 3.5 55.4 1.0
O2A A:ATP505 3.5 41.5 1.0
PG A:ATP505 3.6 45.8 1.0
OD1 A:ASP210 3.7 52.6 1.0
O3B A:ATP505 3.7 33.4 1.0
OG1 A:THR378 3.9 34.8 1.0
O3A A:ATP505 4.1 20.3 1.0
NZ A:LYS19 4.2 48.2 1.0
O2G A:ATP505 4.2 36.3 1.0
CB A:THR378 4.3 28.2 1.0
CG A:ASP210 4.4 45.0 1.0
PA A:ATP505 4.4 43.4 1.0
OD2 A:ASP210 4.5 44.7 1.0
CA A:GLY212 4.7 41.5 1.0
CG A:GLU14 4.7 31.2 1.0
O2B A:ATP505 4.8 43.9 1.0
O1G A:ATP505 4.8 35.4 1.0
CG2 A:THR378 4.9 13.0 1.0

Reference:

T.Nierhaus, S.H.Mclaughlin, F.Burmann, D.Kureisaite-Ciziene, S.L.Maslen, J.M.Skehel, C.W.H.Yu, S.M.V.Freund, L.F.H.Funke, J.W.Chin, J.Lowe. Bacterial Divisome Protein Ftsa Forms Curved Antiparallel Double Filaments When Binding to Ftsn. Nat Microbiol V. 7 1686 2022.
ISSN: ESSN 2058-5276
PubMed: 36123441
DOI: 10.1038/S41564-022-01206-9
Page generated: Thu Oct 3 04:58:26 2024

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