Phosphorus in PDB 1al6: Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate

All present enzymatic activity of Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate:
4.1.3.7;

The structure of Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate, PDB code: 1al6 was solved by K.C.Usher, S.J.Remington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.430, 78.480, 58.450, 90.00, 78.89, 90.00
R / Rfree (%)	15.7 / n/a

The binding sites of Phosphorus atom in the Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate (pdb code 1al6). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate, PDB code: 1al6:
Jump to Phosphorus binding site number: 1; 2; 3;

Phosphorus binding site 1 out of 3 in the Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:P700 b:51.4 occ:1.00 P3B A:HAX700 0.0 51.4 1.0 O7A A:HAX700 1.5 36.4 1.0 O9A A:HAX700 1.5 38.7 1.0 O8A A:HAX700 1.5 75.0 1.0 O3B A:HAX700 1.6 32.1 1.0 C3B A:HAX700 2.7 9.6 1.0 CE A:LYS366 3.4 0.0 0.0 C4B A:HAX700 3.6 9.6 1.0 C2B A:HAX700 3.9 8.6 1.0 O2B A:HAX700 3.9 16.0 1.0 NZ A:LYS366 4.0 75.2 1.0 C1B A:HAX700 4.4 9.6 1.0 O4B A:HAX700 4.6 12.1 1.0 CD A:LYS366 4.6 38.4 1.0 C5B A:HAX700 4.7 14.8 1.0

Phosphorus binding site 2 out of 3 in the Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:P700 b:12.8 occ:1.00 P1A A:HAX700 0.0 12.8 1.0 O2A A:HAX700 1.5 9.3 1.0 O1A A:HAX700 1.5 18.9 1.0 O5B A:HAX700 1.6 19.9 1.0 O3A A:HAX700 1.6 18.6 1.0 C5B A:HAX700 2.6 14.8 1.0 P2A A:HAX700 2.8 14.4 1.0 O5A A:HAX700 3.3 10.4 1.0 O4A A:HAX700 3.5 21.2 1.0 O A:HOH547 3.5 22.9 1.0 O A:HOH539 3.7 14.1 1.0 C4B A:HAX700 3.8 9.6 1.0 CG A:LYS368 3.8 37.3 1.0 O A:HOH623 3.9 22.7 1.0 O6A A:HAX700 4.0 10.4 1.0 O4B A:HAX700 4.0 12.1 1.0 C8A A:HAX700 4.1 16.6 1.0 N A:LYS368 4.1 7.7 1.0 C2B A:HAX700 4.2 8.6 1.0 C3B A:HAX700 4.4 9.6 1.0 CB A:LYS368 4.4 16.2 1.0 CCP A:HAX700 4.6 5.7 1.0 C1B A:HAX700 4.7 9.6 1.0 CA A:ALA367 4.8 9.6 1.0 N9A A:HAX700 4.9 14.1 1.0 CA A:LYS368 4.9 11.2 1.0 O A:LYS366 4.9 17.9 1.0 C A:ALA367 5.0 9.6 1.0

Phosphorus binding site 3 out of 3 in the Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Chicken Citrate Synthase Complex with N-Hydroxyamido-Coa and Oxaloacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:P700 b:14.4 occ:1.00 P2A A:HAX700 0.0 14.4 1.0 O5A A:HAX700 1.5 10.4 1.0 O4A A:HAX700 1.5 21.2 1.0 O3A A:HAX700 1.6 18.6 1.0 O6A A:HAX700 1.6 10.4 1.0 CCP A:HAX700 2.6 5.7 1.0 P1A A:HAX700 2.8 12.8 1.0 O1A A:HAX700 3.2 18.9 1.0 O5B A:HAX700 3.6 19.9 1.0 NH2 A:ARG46 3.7 13.3 1.0 O A:HOH547 3.8 22.9 1.0 O A:HOH623 3.8 22.7 1.0 CBP A:HAX700 3.9 6.9 1.0 NE A:ARG46 3.9 11.0 1.0 O2A A:HAX700 3.9 9.3 1.0 CZ A:ARG46 4.2 10.0 1.0 CAP A:HAX700 4.3 5.8 1.0 CEP A:HAX700 4.3 9.2 1.0 O A:HOH637 4.5 15.0 1.0 CA A:ALA321 4.5 4.8 1.0 OAP A:HAX700 4.7 5.2 1.0 O A:HIS320 4.7 8.5 1.0 O A:HOH539 4.8 14.1 1.0 CB A:ALA321 4.8 6.1 1.0 N A:ALA321 4.9 7.2 1.0 C5B A:HAX700 4.9 14.8 1.0 C A:HIS320 5.0 7.4 1.0

B.Schwartz, K.W.Vogel, K.C.Usher, C.Narasimhan, H.M.Miziorko, S.J.Remington, D.G.Drueckhammer. Mechanisms of Enzyme-Catalyzed Deprotonation of Acetyl-Coenzyme A To Be Published.