Manganese in PDB 4v0x: The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-684)

All present enzymatic activity of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-684):
3.1.3.16;

The structure of The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-684), PDB code: 4v0x 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)	51.337 / 1.85
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.540, 67.540, 158.010, 90.00, 90.00, 90.00
R / Rfree (%)	17.66 / 22.22

The binding sites of Manganese atom in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-684) (pdb code 4v0x). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-684), PDB code: 4v0x:

Manganese binding site 1 out of 1 in the The Crystal Structure of Mouse PP1G in Complex with Truncated Human PPP1R15B (631-684)


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 (631-684) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:26.7 occ:0.76 O A:HOH2036 2.2 35.0 1.0 OD1 A:ASN124 2.2 26.3 1.0 NE2 A:HIS173 2.2 23.8 1.0 OD2 A:ASP92 2.3 28.5 1.0 ND1 A:HIS248 2.3 28.8 1.0 O A:HOH2023 2.3 37.4 1.0 HA A:HIS248 2.9 37.7 1.0 CE1 A:HIS173 3.1 24.0 1.0 CE1 A:HIS248 3.2 28.6 1.0 HE1 A:HIS173 3.2 28.8 1.0 CG A:ASN124 3.2 25.0 1.0 HD2 A:HIS125 3.2 32.1 1.0 CG A:ASP92 3.2 29.6 1.0 HE1 A:HIS248 3.2 34.3 1.0 CD2 A:HIS173 3.3 26.1 1.0 HD22 A:ASN124 3.3 34.0 1.0 CG A:HIS248 3.4 29.1 1.0 HD2 A:HIS173 3.5 31.3 1.0 OD1 A:ASP92 3.6 25.9 1.0 ND2 A:ASN124 3.7 28.4 1.0 O A:HOH2079 3.7 44.6 1.0 CA A:HIS248 3.7 31.4 1.0 HB2 A:HIS248 3.8 36.5 1.0 H A:ASN124 3.8 24.6 1.0 CB A:HIS248 3.8 30.4 1.0 OD2 A:ASP64 4.0 34.3 1.0 CD2 A:HIS125 4.1 26.8 1.0 O A:HOH2049 4.1 42.9 1.0 ND1 A:HIS173 4.3 22.4 1.0 O A:HIS248 4.3 36.5 1.0 O A:HOH2024 4.3 73.7 1.0 NE2 A:HIS248 4.4 28.5 1.0 CG A:HIS173 4.4 23.9 1.0 C A:HIS248 4.5 35.4 1.0 CB A:ASP92 4.5 29.1 1.0 CD2 A:HIS248 4.5 29.0 1.0 HB2 A:ASP92 4.5 34.9 1.0 CB A:ASN124 4.5 24.4 1.0 HD21 A:ASN124 4.5 34.0 1.0 N A:ASN124 4.6 20.5 1.0 H A:HIS125 4.6 28.2 1.0 H A:HIS248 4.6 40.6 1.0 NE2 A:HIS125 4.6 28.9 1.0 HB3 A:ASN124 4.7 29.3 1.0 N A:HIS248 4.7 33.9 1.0 OD1 A:ASP64 4.7 32.7 1.0 CG A:ASP64 4.7 31.8 1.0 HB3 A:ASP92 4.8 34.9 1.0 HB3 A:HIS248 4.8 36.5 1.0 O A:LEU205 4.8 22.7 1.0 NE2 A:HIS66 4.9 33.0 1.0 HE1 A:HIS66 4.9 41.4 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