Zinc in PDB 5lku: Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A.

All present enzymatic activity of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A.:
2.3.1.48;

The structure of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A., PDB code: 5lku was solved by Z.Kaczmarska, E.Ortega, J.A.Marquez, D.Panne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 3.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	93.960, 156.400, 110.680, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.2

The binding sites of Zinc atom in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A. (pdb code 5lku). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A., PDB code: 5lku:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1701 b:0.7 occ:1.00 SG A:CYS1183 2.1 89.3 1.0 SG A:CYS1204 2.2 0.8 1.0 SG A:CYS1201 2.4 75.9 1.0 SG A:CYS1177 2.7 0.9 1.0 CB A:CYS1183 3.1 98.8 1.0 CB A:CYS1204 3.3 0.7 1.0 CB A:CYS1177 3.5 0.2 1.0 CB A:CYS1201 3.6 88.6 1.0 N A:CYS1201 4.3 0.2 1.0 CA A:CYS1183 4.5 0.9 1.0 CA A:CYS1201 4.5 93.6 1.0 CA A:CYS1204 4.6 0.6 1.0 N A:CYS1204 4.7 0.7 1.0 CD A:LYS1180 4.9 0.9 1.0 C A:CYS1183 4.9 0.8 1.0 NZ A:LYS1180 5.0 97.5 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1702 b:70.9 occ:1.00 SG A:CYS1275 2.1 71.6 1.0 SG A:CYS1250 2.2 54.2 1.0 SG A:CYS1247 2.3 58.8 1.0 SG A:CYS1272 2.6 63.4 1.0 CB A:CYS1250 3.1 56.4 1.0 CB A:CYS1247 3.3 62.8 1.0 CB A:CYS1275 3.3 76.9 1.0 N A:CYS1250 3.5 65.7 1.0 CB A:CYS1272 3.6 70.3 1.0 CA A:CYS1250 3.9 59.4 1.0 N A:CYS1272 4.1 64.5 1.0 N A:CYS1275 4.2 76.0 1.0 CA A:CYS1275 4.3 78.9 1.0 CA A:CYS1272 4.4 69.5 1.0 CB A:GLU1249 4.6 76.3 1.0 C A:GLU1249 4.6 70.7 1.0 CA A:CYS1247 4.7 64.4 1.0 C A:CYS1250 4.8 59.5 1.0 O A:CYS1272 4.9 74.0 1.0 N A:GLY1251 4.9 60.0 1.0 CA A:GLU1249 4.9 73.4 1.0 NH1 A:ARG1252 4.9 69.5 1.0 C A:CYS1272 5.0 73.4 1.0 N A:GLU1249 5.0 75.7 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1703 b:59.5 occ:1.00 ND1 A:HIS1255 2.1 49.4 1.0 SG A:CYS1163 2.1 46.4 1.0 SG A:CYS1164 2.1 47.1 1.0 SG A:CYS1258 2.6 48.3 1.0 CE1 A:HIS1255 3.1 50.6 1.0 CG A:HIS1255 3.1 50.4 1.0 CB A:CYS1163 3.3 50.7 1.0 CB A:HIS1255 3.4 52.6 1.0 CB A:CYS1164 3.4 48.1 1.0 CB A:CYS1258 3.5 46.0 1.0 N A:CYS1164 3.5 49.4 1.0 C A:CYS1163 4.0 53.8 1.0 CA A:CYS1164 4.0 47.7 1.0 N A:HIS1255 4.1 52.0 1.0 NE2 A:HIS1255 4.2 52.1 1.0 CD2 A:HIS1255 4.2 51.1 1.0 CA A:CYS1163 4.2 53.3 1.0 O A:CYS1164 4.3 45.5 1.0 CA A:HIS1255 4.4 50.7 1.0 C A:CYS1164 4.4 48.0 1.0 O A:CYS1163 4.6 59.0 1.0 CA A:CYS1258 5.0 46.1 1.0 N A:CYS1163 5.0 54.5 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Coenzyme A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1704 b:95.7 occ:1.00 SG A:CYS1408 2.4 56.5 1.0 NE2 A:HIS1315 2.4 39.5 1.0 CD2 A:HIS1315 3.1 38.5 1.0 CE1 A:HIS1315 3.5 42.1 1.0 CB A:CYS1408 3.8 49.2 1.0 CG A:HIS1315 4.4 39.4 1.0 ND1 A:HIS1315 4.5 41.6 1.0 CA A:CYS1408 4.9 48.5 1.0 N A:CYS1408 5.0 44.6 1.0

Z.Kaczmarska, E.Ortega, A.Goudarzi, H.Huang, S.Kim, J.A.Marquez, Y.Zhao, S.Khochbin, D.Panne. Structure of P300 in Complex with Acyl-Coa Variants. Nat. Chem. Biol. V. 13 21 2017.
ISSN: ESSN 1552-4469
PubMed: 27820805
DOI: 10.1038/NCHEMBIO.2217