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Magnesium in PDB 2zan: Crystal Structure of Mouse SKD1/VPS4B Atp-Form

Protein crystallography data

The structure of Crystal Structure of Mouse SKD1/VPS4B Atp-Form, PDB code: 2zan was solved by M.Inoue, M.Kawasaki, H.Kamikubo, M.Kataoka, R.Kato, T.Yoshimori, S.Wakatsuki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.46 / 3.00
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 75.607, 75.607, 131.678, 90.00, 90.00, 120.00
R / Rfree (%) 22.4 / 26.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mouse SKD1/VPS4B Atp-Form (pdb code 2zan). 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 Crystal Structure of Mouse SKD1/VPS4B Atp-Form, PDB code: 2zan:

Magnesium binding site 1 out of 1 in 2zan

Go back to Magnesium Binding Sites List in 2zan
Magnesium binding site 1 out of 1 in the Crystal Structure of Mouse SKD1/VPS4B Atp-Form


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 Mouse SKD1/VPS4B Atp-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg445

b:47.7
occ:1.00
OG A:SER181 2.3 40.7 1.0
O2B A:ATP446 2.4 59.9 1.0
O3G A:ATP446 2.4 56.8 1.0
OD1 A:ASP234 3.1 84.2 1.0
OD2 A:ASP234 3.5 88.2 1.0
CG A:ASP234 3.5 85.6 1.0
CB A:SER181 3.6 41.9 1.0
PB A:ATP446 3.8 64.8 1.0
PG A:ATP446 3.8 61.1 1.0
OE2 A:GLU235 4.0 82.0 1.0
O3B A:ATP446 4.1 60.5 1.0
OE1 A:GLU235 4.2 79.4 1.0
CD A:GLU235 4.2 81.1 1.0
O1A A:ATP446 4.6 56.4 1.0
N A:SER181 4.6 37.7 1.0
CA A:SER181 4.6 41.0 1.0
O1G A:ATP446 4.7 61.0 1.0
O1B A:ATP446 4.7 52.5 1.0
O3A A:ATP446 4.7 60.6 1.0
CB A:ASP234 4.9 83.5 1.0
O2G A:ATP446 4.9 61.9 1.0

Reference:

M.Inoue, H.Kamikubo, M.Kataoka, R.Kato, T.Yoshimori, S.Wakatsuki, M.Kawasaki. Nucleotide-Dependent Conformational Changes and Assembly of the Aaa Atpase SKD1/VPS4B Traffic V. 9 2180 2008.
ISSN: ISSN 1398-9219
PubMed: 18796009
DOI: 10.1111/J.1600-0854.2008.00831.X
Page generated: Mon Dec 14 07:50:06 2020

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