Strontium in PDB 6e21: Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20

All present enzymatic activity of Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20:
2.7.11.11;

The structure of Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20, PDB code: 6e21 was solved by A.Kovalevsky, O.O.Gerlits, S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.332, 79.898, 100.292, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 27.5

The binding sites of Strontium atom in the Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20 (pdb code 6e21). This binding sites where shown within 5.0 Angstroms radius around Strontium atom.
In total 2 binding sites of Strontium where determined in the Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20, PDB code: 6e21:
Jump to Strontium binding site number: 1; 2;

Strontium binding site 1 out of 2 in the Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 1 of Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20 within 5.0Å range: probe atom residue distance (Å) B Occ A:Sr401 b:20.6 occ:1.00 O1P B:SEP621 2.5 23.1 1.0 D2 A:DOD537 2.6 17.4 1.0 D2 A:DOD624 2.6 43.1 1.0 O2B A:ADP403 2.7 23.5 1.0 OD2 A:ASP184 2.8 18.0 1.0 O A:DOD533 2.8 23.3 1.0 OD1 A:ASP184 2.8 19.4 1.0 O A:DOD624 2.9 42.3 1.0 D1 A:DOD537 3.0 18.3 1.0 O A:DOD537 3.0 20.6 1.0 D1 B:DOD704 3.0 35.9 1.0 HA3 A:GLY186 3.1 15.3 0.9 DA3 A:GLY186 3.1 15.3 0.1 CG A:ASP184 3.2 18.7 1.0 O B:DOD704 3.2 35.5 1.0 D1 A:DOD533 3.4 23.8 1.0 D2 B:DOD703 3.4 12.9 1.0 DZ1 A:LYS72 3.4 20.7 1.0 D2 A:DOD533 3.5 22.9 1.0 D2 B:DOD704 3.5 36.9 1.0 D1 A:DOD624 3.6 45.0 1.0 P B:SEP621 3.8 24.9 1.0 O1B A:ADP403 3.8 20.7 1.0 PB A:ADP403 3.9 22.8 1.0 O3P B:SEP621 3.9 27.6 1.0 D A:GLY186 4.0 17.0 0.5 H A:GLY186 4.0 17.0 0.5 CA A:GLY186 4.2 15.7 1.0 D2 A:DOD595 4.2 38.9 1.0 O B:DOD703 4.2 12.8 1.0 SR A:SR402 4.3 18.5 1.0 D1 B:DOD703 4.3 13.4 1.0 NZ A:LYS72 4.4 20.1 1.0 D1 A:DOD509 4.4 66.4 1.0 N A:GLY186 4.5 16.9 1.0 DOP2 B:SEP621 4.5 19.6 1.0 DA2 A:GLY186 4.6 15.6 0.5 HA2 A:GLY186 4.6 15.6 0.5 OD2 A:ASP166 4.6 21.2 1.0 CB A:ASP184 4.6 16.2 1.0 DZ3 A:LYS72 4.6 19.9 1.0 OG B:SEP621 4.7 26.5 1.0 HB2 B:SEP621 4.8 24.8 1.0 HE1 B:HIS623 4.8 62.2 1.0 O2P B:SEP621 4.8 22.2 1.0 DZ2 A:LYS72 4.9 17.8 1.0 D1 A:DOD595 4.9 40.5 1.0 O3B A:ADP403 4.9 22.8 1.0 DB2 A:ASP184 4.9 17.2 0.4 HB2 A:ASP184 4.9 17.2 0.6 O3A A:ADP403 5.0 22.3 1.0

Strontium binding site 2 out of 2 in the Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 2 of Joint X-Ray/Neutron Structure of Pkac with Products SR2-Adp and Phosphorylated Peptide SP20 within 5.0Å range: probe atom residue distance (Å) B Occ A:Sr402 b:18.5 occ:1.00 D2 B:DOD707 2.5 22.6 1.0 O1A A:ADP403 2.6 17.7 1.0 O1B A:ADP403 2.6 20.7 1.0 OD2 A:ASP184 2.7 18.0 1.0 OD1 A:ASN171 2.7 13.7 1.0 D2 B:DOD703 2.8 12.9 1.0 O B:DOD703 2.8 12.8 1.0 O A:DOD547 2.9 30.0 1.0 O B:DOD707 3.0 22.0 1.0 DD22 A:ASN171 3.4 16.1 0.5 HD22 A:ASN171 3.4 16.1 0.5 D1 A:DOD547 3.4 30.7 1.0 D1 B:DOD703 3.5 13.4 1.0 D2 A:DOD547 3.6 33.2 1.0 DE3 A:LYS168 3.6 17.5 0.2 HE3 A:LYS168 3.6 17.5 0.8 DOP2 B:SEP621 3.6 19.6 1.0 D1 B:DOD707 3.7 23.3 1.0 CG A:ASP184 3.7 18.7 1.0 CG A:ASN171 3.7 16.1 1.0 PB A:ADP403 3.7 22.8 1.0 DZ1 A:LYS168 3.7 19.2 1.0 HZ1 A:LYS168 3.7 19.2 0.0 O1P B:SEP621 3.7 23.1 1.0 DB2 A:ASP184 3.8 17.2 0.4 HB2 A:ASP184 3.8 17.2 0.6 PA A:ADP403 3.9 18.9 1.0 H5'1 A:ADP403 3.9 21.7 1.0 ND2 A:ASN171 4.0 16.1 1.0 CB A:ASP184 4.2 16.2 1.0 HB3 A:ASP184 4.2 17.2 0.3 DB3 A:ASP184 4.2 17.2 0.7 DE2 A:LYS168 4.2 16.7 0.8 HE2 A:LYS168 4.2 16.7 0.2 O3A A:ADP403 4.2 22.3 1.0 O2B A:ADP403 4.2 23.5 1.0 SR A:SR401 4.3 20.6 1.0 CE A:LYS168 4.3 18.2 1.0 D2 A:DOD501 4.4 68.3 1.0 D1 A:DOD537 4.5 18.3 1.0 NZ A:LYS168 4.5 18.4 1.0 OD2 A:ASP166 4.6 21.2 1.0 O2P B:SEP621 4.6 22.2 1.0 OD1 A:ASP184 4.7 19.4 1.0 C5' A:ADP403 4.8 20.8 1.0 DA A:ASN171 4.8 13.9 1.0 O2A A:ADP403 4.8 20.1 1.0 O A:DOD501 4.8 67.9 1.0 P B:SEP621 4.9 24.9 1.0 DD21 A:ASN171 4.9 17.0 0.7 HD21 A:ASN171 4.9 17.0 0.3 O5' A:ADP403 4.9 22.0 1.0 O B:DOD718 4.9 42.9 1.0 D1 B:DOD718 5.0 42.6 1.0 HB2 B:SEP621 5.0 24.8 1.0 DB3 A:GLU170 5.0 17.5 0.3 HB3 A:GLU170 5.0 17.5 0.7 O3' A:ADP403 5.0 24.1 1.0 DO3' A:ADP403 5.0 26.6 1.0

O.Gerlits, K.L.Weiss, M.P.Blakeley, G.Veglia, S.S.Taylor, A.Kovalevsky. Zooming in on Protons: Neutron Structure of Protein Kinase A Trapped in A Product Complex. Sci Adv V. 5 V0482 2019.
ISSN: ESSN 2375-2548
PubMed: 30906862
DOI: 10.1126/SCIADV.AAV0482