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Magnesium in PDB 2c43: Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A

Enzymatic activity of Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A

All present enzymatic activity of Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A:
1.2.1.31;

Protein crystallography data

The structure of Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A, PDB code: 2c43 was solved by G.Bunkoczi, X.Wu, E.Dubinina, C.Johansson, C.Smee, A.Turnbull, F.Von Delft, C.Arrowsmith, A.Edwards, M.Sundstrom, J.Weigelt, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.39 / 1.93
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.589, 68.957, 70.745, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 21.9

Other elements in 2c43:

The structure of Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A (pdb code 2c43). 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 Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A, PDB code: 2c43:

Magnesium binding site 1 out of 1 in 2c43

Go back to Magnesium Binding Sites List in 2c43
Magnesium binding site 1 out of 1 in the Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1317

b:18.9
occ:1.00
 OE2 A:GLU191 2.1 25.4 1.0
OD1 A:ASP139 2.1 9.9 1.0
O A:HOH2176 2.2 15.5 1.0
O4A A:COA1316 2.2 11.6 1.0
O2A A:COA1316 2.4 5.8 1.0
CD A:GLU191 3.0 18.7 1.0
CE A:MET141 3.1 36.2 1.0
CG A:ASP139 3.1 4.3 1.0
OD2 A:ASP139 3.3 8.9 1.0
P1A A:COA1316 3.5 7.0 1.0
P2A A:COA1316 3.5 14.2 1.0
OE1 A:GLU191 3.6 25.2 1.0
O3A A:COA1316 3.8 15.9 1.0
CG A:GLU191 4.0 30.0 1.0
OG A:SER120 4.0 10.7 1.0
O A:HOH2065 4.2 27.2 1.0
O1A A:COA1316 4.3 9.8 1.0
CCP A:COA1316 4.4 24.8 1.0
O A:HOH2102 4.4 26.2 1.0
CB A:ASP139 4.5 9.1 1.0
O A:ILE140 4.5 15.2 1.0
O6A A:COA1316 4.5 15.4 1.0
O5A A:COA1316 4.6 11.3 1.0
NZ A:LYS195 4.7 2.3 1.0
SD A:MET141 4.7 23.5 1.0
O5B A:COA1316 4.7 11.1 1.0
CB A:GLU191 4.8 13.7 1.0
CA A:ASP139 5.0 6.9 1.0
NE1 A:TRP187 5.0 19.0 1.0

Reference:

G.Bunkoczi, S.Pasta, A.Joshi, X.Wu, K.L.Kavanagh, S.Smith, U.Oppermann. Mechanism and Substrate Recognition of Human Holo Acp Synthase. Chem. Biol. V. 14 1243 2007.
ISSN: ISSN 1074-5521
PubMed: 18022563
DOI: 10.1016/J.CHEMBIOL.2007.10.013
Page generated: Mon Dec 14 07:18:20 2020

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