Manganese in PDB 4v0v: The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660)

All present enzymatic activity of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660):
3.1.3.16;

The structure of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660), PDB code: 4v0v was solved by R.Chen, Y.Yan, A.C.Casado, D.Ron, R.J.Read, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.263 / 1.61
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.800, 67.890, 156.380, 90.00, 90.00, 90.00
R / Rfree (%)	17.63 / 20.29

The structure of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660) also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Manganese atom in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660) (pdb code 4v0v). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660), PDB code: 4v0v:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:13.7 occ:0.95 OD1 A:ASN124 2.1 12.2 1.0 O A:HOH2061 2.2 19.2 1.0 OD2 A:ASP92 2.2 14.4 1.0 O A:HOH2085 2.2 19.3 1.0 NE2 A:HIS173 2.2 13.2 1.0 ND1 A:HIS248 2.3 12.3 1.0 CG A:ASN124 3.1 14.3 1.0 CE1 A:HIS248 3.2 14.4 1.0 CG A:ASP92 3.2 16.1 1.0 CE1 A:HIS173 3.2 13.3 1.0 CD2 A:HIS173 3.2 11.8 1.0 O A:HOH2171 3.4 28.1 1.0 CG A:HIS248 3.4 11.1 1.0 OD1 A:ASP92 3.6 13.3 1.0 ND2 A:ASN124 3.6 16.6 1.0 CA A:HIS248 3.7 11.2 1.0 O A:HOH2060 3.8 32.4 1.0 CB A:HIS248 3.9 14.0 1.0 OD2 A:ASP64 4.0 19.4 1.0 CD2 A:HIS125 4.1 14.8 1.0 O A:HOH2104 4.2 39.7 1.0 ND1 A:HIS173 4.3 12.7 1.0 NE2 A:HIS248 4.4 15.4 1.0 CG A:HIS173 4.4 13.4 1.0 O A:HIS248 4.4 19.1 1.0 CB A:ASP92 4.5 15.8 1.0 CB A:ASN124 4.5 12.1 1.0 CD2 A:HIS248 4.5 11.8 1.0 N A:ASN124 4.5 12.0 1.0 C A:HIS248 4.5 14.0 1.0 N A:HIS248 4.7 12.8 1.0 NE2 A:HIS125 4.7 19.8 1.0 OD1 A:ASP64 4.7 19.5 1.0 CG A:ASP64 4.8 18.5 1.0 O A:LEU205 4.9 12.3 1.0

Manganese binding site 2 out of 2 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-660) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn302 b:12.8 occ:0.99 OD1 C:ASN124 2.2 11.7 1.0 OD2 C:ASP92 2.2 13.7 1.0 O C:HOH2050 2.2 16.0 1.0 NE2 C:HIS173 2.2 13.0 1.0 O C:HOH2073 2.2 17.5 1.0 ND1 C:HIS248 2.3 11.2 1.0 CE1 C:HIS248 3.2 11.9 1.0 CE1 C:HIS173 3.2 13.1 1.0 CD2 C:HIS173 3.2 12.6 1.0 CG C:ASP92 3.2 16.4 1.0 CG C:ASN124 3.2 13.2 1.0 O C:HOH2154 3.4 26.2 1.0 CG C:HIS248 3.5 12.2 1.0 OD1 C:ASP92 3.6 12.8 1.0 ND2 C:ASN124 3.7 13.4 1.0 CA C:HIS248 3.7 11.7 1.0 CB C:HIS248 3.9 9.4 1.0 OD2 C:ASP64 4.0 19.9 1.0 O C:HOH2049 4.0 32.9 1.0 CD2 C:HIS125 4.1 15.5 1.0 O C:HOH2155 4.2 37.6 1.0 ND1 C:HIS173 4.3 12.2 1.0 CG C:HIS173 4.3 12.1 1.0 NE2 C:HIS248 4.3 11.7 1.0 CB C:ASP92 4.4 15.3 1.0 O C:HIS248 4.5 17.8 1.0 CD2 C:HIS248 4.5 10.6 1.0 CB C:ASN124 4.5 14.0 1.0 N C:ASN124 4.5 12.0 1.0 C C:HIS248 4.6 14.0 1.0 N C:HIS248 4.7 11.6 1.0 OD1 C:ASP64 4.7 18.6 1.0 NE2 C:HIS125 4.7 17.6 1.0 CG C:ASP64 4.8 17.2 1.0 O C:LEU205 4.8 12.3 1.0 NE2 C:HIS66 5.0 23.7 1.0

R.Chen, C.Rato, Y.Yan, A.Crespillo-Casado, H.J.Clarke, H.P.Harding, S.J.Marciniak, R.J.Read, D.Ron. G-Actin Provides Substrate-Specificity to Eukaryotic Initiation Factor 2ALPHA Holophosphatases. Elife V. 4 2015.
ISSN: ISSN 2050-084X
PubMed: 25774600
DOI: 10.7554/ELIFE.04871