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Magnesium in PDB 5d9c: Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data)

Protein crystallography data

The structure of Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data), PDB code: 5d9c was solved by K.Yamashita, D.Pan, T.Okuda, T.Murai, A.Kodan, T.Yamaguchi, K.Gomi, N.Kajiyama, H.Kato, H.Ago, M.Yamamoto, T.Nakatsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.71 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.100, 77.500, 84.800, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.5

Other elements in 5d9c:

The structure of Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data) also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data) (pdb code 5d9c). 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 Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data), PDB code: 5d9c:

Magnesium binding site 1 out of 1 in 5d9c

Go back to Magnesium Binding Sites List in 5d9c
Magnesium binding site 1 out of 1 in the Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Luciferin-Regenerating Enzyme Solved By Siras Using Xfel (Refined Against Hg Derivative Data) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:19.3
occ:1.00
OE1 A:GLU18 2.0 18.8 1.0
OD1 A:ASP212 2.0 17.2 1.0
OD1 A:ASN160 2.0 21.4 1.0
O A:HOH551 2.1 20.2 1.0
O A:HOH529 2.2 21.1 1.0
O A:HOH619 2.3 21.2 1.0
CD A:GLU18 3.0 19.5 1.0
CG A:ASN160 3.0 21.5 1.0
CG A:ASP212 3.1 21.9 1.0
OE2 A:GLU18 3.4 20.9 1.0
ND2 A:ASN160 3.4 22.9 1.0
OD2 A:ASP212 3.6 21.9 1.0
O A:HOH524 3.6 23.7 1.0
O4 A:MPD402 4.0 26.5 1.0
ND2 A:ASN110 4.1 19.6 1.0
O A:THR255 4.2 18.5 1.0
CG A:GLU18 4.2 17.9 1.0
N A:GLY213 4.3 18.0 1.0
CB A:ASN160 4.3 20.9 1.0
OD2 A:ASP111 4.3 19.3 1.0
C A:ASP212 4.4 20.1 1.0
CB A:ASP212 4.4 18.4 1.0
O A:HOH550 4.5 22.5 1.0
CG A:ASP111 4.6 22.3 1.0
CB A:ASP111 4.6 16.4 1.0
O A:HOH517 4.6 32.8 1.0
CA A:ASP212 4.6 16.1 1.0
OD1 A:ASN110 4.7 25.0 1.0
CG A:ASN110 4.8 22.3 1.0
CA A:GLY213 4.8 17.7 1.0
O A:ASP212 4.8 19.2 1.0
CA A:ASN160 4.8 19.0 1.0

Reference:

K.Yamashita, D.Pan, T.Okuda, M.Sugahara, A.Kodan, T.Yamaguchi, T.Murai, K.Gomi, N.Kajiyama, E.Mizohata, M.Suzuki, E.Nango, K.Tono, Y.Joti, T.Kameshima, J.Park, C.Song, T.Hatsui, M.Yabashi, S.Iwata, H.Kato, H.Ago, M.Yamamoto, T.Nakatsu. An Isomorphous Replacement Method For Efficient De Novo Phasing For Serial Femtosecond Crystallography. Sci Rep V. 5 14017 2015.
ISSN: ESSN 2045-2322
PubMed: 26360462
DOI: 10.1038/SREP14017
Page generated: Sun Sep 29 02:38:21 2024

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