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Chlorine 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:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Aminoadipate-Semialdehyde Dehydrogenase- Phosphopantetheinyl Transferase in Complex with Coenzyme A, PDB code: 2c43:

Chlorine binding site 1 out of 1 in 2c43

Go back to Chlorine Binding Sites List in 2c43
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl1318

b:10.1
occ:1.00
 NH2 A:ARG74 3.1 3.9 1.0
NE A:ARG74 3.2 5.1 1.0
N A:GLN51 3.4 10.9 1.0
NH1 A:ARG78 3.5 6.5 1.0
CZ A:ARG74 3.6 8.6 1.0
CG A:GLU54 3.8 15.7 1.0
CB A:GLN51 3.8 9.7 1.0
CD A:ARG78 3.8 7.8 1.0
CB A:ILE50 3.9 9.0 1.0
CG A:GLN51 3.9 8.6 1.0
CD A:GLN51 4.0 7.3 1.0
CD1 A:LEU94 4.1 15.4 1.0
CA A:ILE50 4.1 2.0 1.0
CB A:GLU54 4.2 9.0 1.0
CB A:ARG74 4.2 12.1 1.0
CA A:GLN51 4.2 9.7 1.0
C A:ILE50 4.2 6.3 1.0
OE1 A:GLN51 4.3 9.8 1.0
CZ A:ARG78 4.3 11.8 1.0
CG2 A:ILE50 4.4 10.2 1.0
CG A:ARG74 4.4 10.4 1.0
CG A:ARG78 4.4 7.5 1.0
CD A:ARG74 4.4 4.3 1.0
NE A:ARG78 4.5 9.8 1.0
NE2 A:GLN51 4.5 9.8 1.0
O A:ARG74 5.0 9.8 1.0
NH1 A:ARG74 5.0 7.7 1.0
CD A:GLU54 5.0 22.9 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: Thu Jul 10 21:39:18 2025

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