Manganese in PDB 1zp9: Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions.

The structure of Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions., PDB code: 1zp9 was solved by A.Wlodawer, N.Laronde-Leblanc, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.306, 80.373, 121.320, 90.00, 90.02, 90.00
R / Rfree (%)	17.7 / 24.9

The binding sites of Manganese atom in the Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions. (pdb code 1zp9). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions., PDB code: 1zp9:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn259 b:16.9 occ:1.00 O A:HOH1858 1.8 25.9 1.0 O2A A:ATP260 2.0 15.2 1.0 OD2 A:ASP212 2.1 19.8 1.0 O A:HOH1229 2.2 25.3 1.0 O1B A:ATP260 2.2 20.6 1.0 OD1 A:ASN201 2.3 12.7 1.0 CG A:ASP212 3.1 16.9 1.0 CG A:ASN201 3.2 15.3 1.0 PA A:ATP260 3.3 15.7 1.0 PB A:ATP260 3.4 15.5 1.0 ND2 A:ASN201 3.5 11.9 1.0 O3A A:ATP260 3.5 17.4 1.0 CB A:ASP212 3.5 16.5 1.0 O A:HOH1741 3.8 43.7 1.0 OD1 A:ASP212 4.1 18.2 1.0 O1A A:ATP260 4.2 14.3 1.0 O A:HOH1387 4.3 25.2 1.0 O3G A:ATP260 4.3 24.5 0.5 O2B A:ATP260 4.4 16.1 1.0 O A:TYR200 4.4 14.7 1.0 O3B A:ATP260 4.4 19.3 1.0 O5' A:ATP260 4.5 16.2 1.0 O2G A:ATP260 4.5 25.1 0.5 CB A:ASN201 4.6 13.2 1.0 PG A:ATP260 4.7 22.1 0.5 C5' A:ATP260 4.8 14.8 1.0 CA A:ASN201 5.0 13.6 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn259 b:14.8 occ:1.00 OD2 B:ASP212 2.0 13.8 1.0 O B:HOH1805 2.0 19.8 1.0 O2A B:ATP260 2.1 13.1 1.0 O1B B:ATP260 2.1 19.8 1.0 OD1 B:ASN201 2.2 16.2 1.0 O B:HOH1140 2.2 24.5 1.0 CG B:ASP212 3.1 14.9 1.0 CG B:ASN201 3.2 14.6 1.0 PB B:ATP260 3.3 15.0 1.0 PA B:ATP260 3.3 13.5 1.0 ND2 B:ASN201 3.5 13.1 1.0 O3A B:ATP260 3.5 12.0 1.0 CB B:ASP212 3.6 14.2 1.0 O2G B:ATP260 3.8 26.1 0.5 O A:HOH1285 4.0 27.4 1.0 O A:HOH1249 4.1 33.1 1.0 OD1 B:ASP212 4.1 13.6 1.0 O1A B:ATP260 4.3 12.4 1.0 O2B B:ATP260 4.3 14.3 1.0 O3B B:ATP260 4.3 21.1 1.0 O B:TYR200 4.5 13.9 1.0 O5' B:ATP260 4.5 13.5 1.0 CB B:ASN201 4.5 13.1 1.0 PG B:ATP260 4.6 23.4 0.5 C5' B:ATP260 4.8 15.0 1.0 CA B:ASN201 4.9 13.0 1.0 OD2 B:ASP196 5.0 22.0 1.0 O3' B:ATP260 5.0 19.2 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn259 b:19.3 occ:1.00 O1B C:ATP260 2.2 22.1 1.0 O2A C:ATP260 2.2 12.7 1.0 O C:HOH1784 2.2 23.9 1.0 OD1 C:ASN201 2.3 14.4 1.0 OD2 C:ASP212 2.3 13.9 1.0 O C:HOH1338 2.3 18.5 1.0 CG C:ASP212 3.2 15.4 1.0 CG C:ASN201 3.2 16.0 1.0 PA C:ATP260 3.3 12.6 1.0 PB C:ATP260 3.3 18.8 1.0 O3A C:ATP260 3.4 16.4 1.0 ND2 C:ASN201 3.5 16.5 1.0 CB C:ASP212 3.6 17.0 1.0 O C:HOH1334 4.0 27.2 1.0 O C:HOH1601 4.1 33.9 1.0 OD1 C:ASP212 4.2 15.3 1.0 O1A C:ATP260 4.2 12.2 1.0 O2B C:ATP260 4.3 22.2 1.0 O3B C:ATP260 4.5 21.3 1.0 O C:TYR200 4.5 17.8 1.0 CB C:ASN201 4.6 14.0 1.0 O5' C:ATP260 4.6 13.8 1.0 O1G C:ATP260 4.6 19.4 0.5 O3G C:ATP260 4.7 27.8 0.5 C5' C:ATP260 4.7 14.3 1.0 PG C:ATP260 4.8 29.5 0.5 CA C:ASN201 4.9 14.8 1.0 OD1 C:ASP196 5.0 29.4 1.0 CA C:ASP212 5.0 17.7 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Full-Legnth A.Fulgidus RIO1 Serine Kinase Bound to Atp and MN2+ Ions. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn259 b:19.9 occ:1.00 O D:HOH1899 2.1 15.8 1.0 OD1 D:ASN201 2.1 17.7 1.0 OD2 D:ASP212 2.2 17.0 1.0 O2A D:ATP260 2.2 12.8 1.0 O D:HOH1115 2.2 24.4 1.0 O1B D:ATP260 2.3 19.8 1.0 CG D:ASN201 3.1 17.0 1.0 CG D:ASP212 3.2 17.3 1.0 ND2 D:ASN201 3.3 11.9 1.0 O D:HOH1200 3.4 23.1 1.0 PA D:ATP260 3.4 12.1 1.0 PB D:ATP260 3.4 15.7 1.0 O3A D:ATP260 3.6 13.8 1.0 CB D:ASP212 3.6 18.0 1.0 O D:HOH1475 4.2 26.2 1.0 OD1 D:ASP212 4.3 18.3 1.0 O1A D:ATP260 4.3 13.1 1.0 O2B D:ATP260 4.3 16.8 1.0 O D:TYR200 4.3 19.4 1.0 O D:HOH1614 4.3 32.4 1.0 CB D:ASN201 4.5 16.2 1.0 O5' D:ATP260 4.6 15.2 1.0 OE2 C:GLU249 4.7 28.8 1.0 O3B D:ATP260 4.7 18.8 1.0 O3G D:ATP260 4.7 17.2 0.5 O D:HOH1283 4.8 27.6 1.0 C5' D:ATP260 4.8 14.6 1.0 CA D:ASN201 4.8 17.3 1.0 OD1 D:ASP196 4.9 23.6 1.0

N.Laronde-Leblanc, T.Guszczynski, T.Copeland, A.Wlodawer. Structure and Activity of the Atypical Serine Kinase RIO1. Febs J. V. 272 3698 2005.
ISSN: ISSN 1742-464X
PubMed: 16008568
DOI: 10.1111/J.1742-4658.2005.04796.X