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Magnesium in PDB 1o6b: Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp

Enzymatic activity of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp

All present enzymatic activity of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp:
2.7.7.3;

Protein crystallography data

The structure of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp, PDB code: 1o6b was solved by Structural Genomix, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.01 / 2.20
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 115.420, 115.420, 115.420, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 27.5

Other elements in 1o6b:

The structure of Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp (pdb code 1o6b). 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 Phosphopantetheine Adenylyltransferase with Adp, PDB code: 1o6b:

Magnesium binding site 1 out of 1 in 1o6b

Go back to Magnesium Binding Sites List in 1o6b
Magnesium binding site 1 out of 1 in the Crystal Structure of Phosphopantetheine Adenylyltransferase with Adp


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 Phosphopantetheine Adenylyltransferase with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg171

b:19.2
occ:0.50
 O A:HOH218 2.1 30.1 1.0
O A:HOH174 2.3 19.7 1.0
OD1 A:ASP139 2.5 22.3 1.0
CG A:ASP139 3.8 25.2 1.0
O A:HOH185 3.9 30.8 1.0
CA A:ASP139 4.3 23.7 1.0
O A:ASP139 4.3 24.6 1.0
O A:HOH250 4.4 43.3 1.0
O A:HOH177 4.4 20.4 1.0
C A:ASP139 4.5 24.3 1.0
OD2 A:ASP139 4.5 25.6 1.0
CB A:ASP139 4.6 23.4 1.0
O A:GLY140 4.7 23.6 1.0
CG A:GLN155 4.9 19.3 1.0
O A:HOH192 4.9 29.0 1.0
O A:HOH219 5.0 40.5 1.0

Reference:

J.Badger, J.M.Sauder, J.M.Adams, S.Antonysamy, K.Bain, M.G.Bergseid, S.G.Buchanan, M.D.Buchanan, Y.Batiyenko, J.A.Christopher, S.Emtage, A.Eroshkina, I.Feil, E.B.Furlong, K.S.Gajiwala, X.Gao, D.He, J.Hendle, A.Huber, K.Hoda, P.Kearins, C.Kissinger, B.Laubert, H.A.Lewis, J.Lin, K.Loomis, D.Lorimer, G.Louie, M.Maletic, C.D.Marsh, I.Miller, J.Molinari, H.J.Muller-Dieckmann, J.M.Newman, B.W.Noland, B.Pagarigan, F.Park, T.S.Peat, K.W.Post, S.Radojicic, A.Ramos, R.Romero, M.E.Rutter, W.E.Sanderson, K.D.Schwinn, J.Tresser, J.Winhoven, T.A.Wright, L.Wu, J.Xu, T.J.Harris. Structural Analysis of A Set of Proteins Resulting From A Bacterial Genomics Project Proteins V. 60 787 2005.
ISSN: ISSN 0887-3585
PubMed: 16021622
DOI: 10.1002/PROT.20541
Page generated: Tue Aug 13 10:33:19 2024

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