Calcium in PDB 4ruk: Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa

All present enzymatic activity of Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa:
2.7.7.3;

The structure of Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa, PDB code: 4ruk was solved by R.Chatterjee, S.Datta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.13 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	79.603, 89.483, 79.616, 90.00, 97.93, 90.00
R / Rfree (%)	20.4 / 25.4

The binding sites of Calcium atom in the Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa (pdb code 4ruk). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa, PDB code: 4ruk:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca203 b:64.4 occ:0.97 O9A E:COA202 2.3 64.7 0.5 O7A E:COA202 2.4 64.9 0.5 O1A E:COA202 2.7 42.5 0.5 NE2 E:HIS17 3.5 40.7 1.0 NH2 E:ARG90 3.5 61.2 1.0 P3B E:COA202 3.6 64.3 0.5 CB E:SER128 3.6 48.7 1.0 C5B E:COA202 3.6 59.2 0.5 P3B E:COA202 3.7 63.2 0.5 CE1 E:HIS17 3.7 34.8 1.0 O3B E:COA202 3.8 64.7 0.5 P1A E:COA202 3.8 51.6 0.5 O9A E:COA202 3.8 59.8 0.5 O5B E:COA202 3.9 53.8 0.5 N E:SER128 3.9 46.1 1.0 C4B E:COA202 4.2 62.4 0.5 C3B E:COA202 4.3 63.2 0.5 O E:HOH303 4.3 33.8 1.0 O8A E:COA202 4.4 60.8 0.5 CA E:SER128 4.4 45.8 1.0 O2A E:COA202 4.5 37.8 0.5 C4B E:COA202 4.5 61.7 0.5 C3B E:COA202 4.6 65.2 0.5 O3B E:COA202 4.6 67.1 0.5 OG E:SER128 4.6 48.2 1.0 O7A E:COA202 4.6 63.6 0.5 CD2 E:HIS17 4.7 38.7 1.0 O8A E:COA202 4.7 61.3 0.5 CZ E:ARG90 4.8 68.9 1.0 ND1 E:HIS17 4.9 34.9 1.0 C E:SER127 5.0 53.3 1.0 O5B E:COA202 5.0 54.4 0.5 O E:ILE126 5.0 55.5 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Phosphoapantetheine Adenylyltransferase Ppat/Coad with Coa and Pyrophosphate From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ F:Ca203 b:66.0 occ:1.00 O7A F:COA201 2.4 63.7 0.5 O9A F:COA201 2.4 63.5 0.5 O1A F:COA201 2.8 47.5 0.5 O F:HOH314 3.1 46.0 1.0 O3B F:COA201 3.2 63.9 0.5 OG F:SER128 3.3 61.0 1.0 P3B F:COA201 3.3 63.6 0.5 NE2 F:HIS17 3.4 40.2 1.0 CE1 F:HIS17 3.6 35.8 1.0 C5B F:COA201 3.7 59.1 0.5 P3B F:COA201 3.7 63.0 0.5 N F:SER128 3.8 45.5 1.0 CB F:SER128 3.8 46.5 1.0 O5B F:COA201 3.9 59.5 0.5 P1A F:COA201 3.9 52.3 0.5 O9A F:COA201 4.0 60.6 0.5 C4B F:COA201 4.2 62.6 0.5 C3B F:COA201 4.2 64.1 0.5 O8A F:COA201 4.2 60.0 0.5 O2A F:COA201 4.4 38.6 0.5 O7A F:COA201 4.5 63.9 0.5 CA F:SER128 4.5 45.6 1.0 O F:HOH305 4.5 39.9 1.0 C4B F:COA201 4.5 61.4 0.5 NH1 F:ARG90 4.6 82.0 1.0 C3B F:COA201 4.6 65.8 0.5 CD2 F:HIS17 4.6 36.2 1.0 O3B F:COA201 4.6 66.3 0.5 O8A F:COA201 4.7 64.0 0.5 ND1 F:HIS17 4.8 35.4 1.0 C F:SER127 4.8 48.1 1.0 CA F:SER127 4.9 49.9 1.0 O F:ILE126 4.9 55.4 1.0

R.Chatterjee, A.Mondal, A.Basu, S.Datta. Transition of Phosphopantetheine Adenylyltransferase From Catalytic to Allosteric State Is Characterized By Ternary Complex Formation in Pseudomonas Aeruginosa Biochim.Biophys.Acta V.1864 773 2016.
ISSN: ISSN 0006-3002
PubMed: 27041211
DOI: 10.1016/J.BBAPAP.2016.03.018