Magnesium in PDB 8qfg: Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination

The structure of Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination, PDB code: 8qfg was solved by A.Chretien, M.F.Nagel, S.Botha, R.De Wijn, L.Brings, K.Doerner, H.Han, J.C.P.Koliyadu, R.Letrun, A.Round, T.Sato, C.Schmidt, R.Secareanu, D.Vonstetten, M.Vakili, A.Wrona, R.Bean, A.Mancuso, J.Schulz, A.R.Pearson, T.Kottke, K.Lorenzen, R.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.08 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.511, 141.425, 104.732, 90, 90, 90
R / Rfree (%)	21 / 23

The binding sites of Magnesium atom in the Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination (pdb code 8qfg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination, PDB code: 8qfg:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:30.4 occ:1.00 OD1 A:ASP156 2.0 33.4 1.0 OD2 A:ASP200 2.1 29.3 1.0 O2B A:ATP402 2.1 34.3 1.0 O2A A:ATP402 2.2 32.5 1.0 O A:ILE157 2.2 30.7 1.0 O3G A:ATP402 2.2 33.5 1.0 CG A:ASP200 3.1 31.2 1.0 CG A:ASP156 3.1 35.2 1.0 HH21 A:ARG283 3.1 40.4 1.0 PB A:ATP402 3.3 37.4 1.0 C A:ILE157 3.4 36.4 1.0 PA A:ATP402 3.4 33.1 1.0 OD1 A:ASP200 3.4 30.8 1.0 PG A:ATP402 3.4 35.1 1.0 H5'1 A:ATP402 3.4 37.7 1.0 O3A A:ATP402 3.6 40.7 1.0 O3B A:ATP402 3.6 44.5 1.0 OD2 A:ASP156 3.6 34.9 1.0 O A:HOH528 3.6 36.5 1.0 H A:PHE160 3.6 41.2 1.0 MG A:MG404 3.7 34.9 1.0 HB3 A:PHE160 3.7 47.2 1.0 H A:ILE157 3.8 34.5 1.0 N A:ILE157 3.8 28.7 1.0 NH2 A:ARG283 3.8 33.6 1.0 HB A:ILE157 3.9 35.6 1.0 HH22 A:ARG283 3.9 40.4 1.0 CA A:ILE157 4.0 30.8 1.0 H A:SER159 4.2 46.7 1.0 C A:ASP156 4.2 32.5 1.0 HA A:VAL158 4.2 37.8 1.0 O1G A:ATP402 4.2 35.9 1.0 HB2 A:PHE160 4.2 47.2 1.0 C5' A:ATP402 4.2 31.4 1.0 O5' A:ATP402 4.3 34.2 1.0 CB A:ASP156 4.3 31.6 1.0 CB A:PHE160 4.4 39.4 1.0 CB A:ASP200 4.4 31.7 1.0 N A:VAL158 4.4 30.8 1.0 CB A:ILE157 4.4 29.7 1.0 O1A A:ATP402 4.5 36.1 1.0 HG22 A:ILE157 4.5 38.7 1.0 N A:PHE160 4.5 34.3 1.0 O2G A:ATP402 4.5 33.2 1.0 HB2 A:ASP200 4.5 38.0 1.0 HB3 A:ASP156 4.6 37.9 1.0 N A:SER159 4.6 38.9 1.0 O1B A:ATP402 4.6 36.9 1.0 H5'2 A:ATP402 4.6 37.7 1.0 O A:ASP156 4.7 34.4 1.0 CA A:VAL158 4.7 31.5 1.0 CA A:ASP156 4.7 29.1 1.0 HA A:ASP156 4.8 35.0 1.0 O A:HOH564 4.8 45.2 1.0 HB3 A:ASP200 4.8 38.0 1.0 HE A:ARG283 4.8 41.8 1.0 C A:VAL158 4.9 32.8 1.0 HA A:ILE157 4.9 37.0 1.0 O A:HOH562 5.0 35.8 1.0

Magnesium binding site 2 out of 2 in the Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac After 5 Seconds of Blue Light Illumination within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:34.9 occ:1.00 O A:HOH536 2.3 35.1 1.0 OD1 A:ASP200 2.3 30.8 1.0 O2A A:ATP402 2.4 32.5 1.0 O A:HOH562 2.4 35.8 1.0 OD2 A:ASP156 2.4 34.9 1.0 O4' A:ATP402 3.2 31.8 1.0 CG A:ASP156 3.2 35.2 1.0 PA A:ATP402 3.4 33.1 1.0 CG A:ASP200 3.4 31.2 1.0 H5'1 A:ATP402 3.4 37.7 1.0 OD1 A:ASP156 3.5 33.4 1.0 O A:HOH528 3.5 36.5 1.0 O5' A:ATP402 3.6 34.2 1.0 HB2 A:CYS201 3.6 39.6 1.0 H A:ASP200 3.7 36.5 1.0 MG A:MG403 3.7 30.4 1.0 O1A A:ATP402 3.7 36.1 1.0 OD2 A:ASP200 3.8 29.3 1.0 C5' A:ATP402 3.9 31.4 1.0 H8 A:ATP402 4.0 40.1 1.0 O A:HOH543 4.1 39.7 1.0 C8 A:ATP402 4.1 33.4 1.0 HB3 A:CYS201 4.1 39.6 1.0 C4' A:ATP402 4.1 31.3 1.0 N9 A:ATP402 4.1 33.0 1.0 C1' A:ATP402 4.2 33.1 1.0 CB A:CYS201 4.3 33.0 1.0 O A:ILE198 4.4 33.1 1.0 H1' A:ATP402 4.4 39.8 1.0 N A:ASP200 4.5 30.4 1.0 CB A:ASP156 4.6 31.6 1.0 HB2 A:ASP156 4.6 37.9 1.0 H4' A:ATP402 4.6 37.6 1.0 CB A:ASP200 4.6 31.7 1.0 N7 A:ATP402 4.7 33.0 1.0 O3A A:ATP402 4.7 40.7 1.0 C4 A:ATP402 4.7 31.1 1.0 C A:ASP200 4.8 33.8 1.0 N A:CYS201 4.8 29.5 1.0 O3G A:ATP402 4.8 33.5 1.0 H5'2 A:ATP402 4.8 37.7 1.0 HA3 A:GLY199 4.8 39.9 1.0 CA A:ASP200 4.9 29.4 1.0 H A:CYS201 4.9 35.4 1.0 C5 A:ATP402 5.0 33.6 1.0

A.Chretien, M.F.Nagel, S.Botha, R.De Wijn, L.Brings, K.Doerner, H.Han, J.C.P.Koliyadu, R.Letrun, A.Round, T.Sato, C.Schmidt, R.Secareanu, D.Von Stetten, M.Vakili, A.Wrona, R.Bean, A.Mancuso, J.Schulz, A.R.Pearson, T.Kottke, K.Lorenzen, R.Schubert. Light-Induced Trpin/Metout Switching During Bluf Domain Activation in Atp-Bound Photoactivatable Adenylate Cyclase Oapac To Be Published.