Magnesium in PDB 8qff: Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac with Atp Bound

The structure of Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac with Atp Bound, PDB code: 8qff 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)	60.04 / 2.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	54.455, 146.435, 104.92, 90, 90, 90
R / Rfree (%)	18.7 / 21.9

The binding sites of Magnesium atom in the Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac with Atp Bound (pdb code 8qff). 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 with Atp Bound, PDB code: 8qff:
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 with Atp Bound


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 with Atp Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:38.0 occ:1.00 OD1 A:ASP156 2.1 57.5 1.0 O2A A:ATP402 2.1 44.7 1.0 O2B A:ATP402 2.1 46.1 1.0 O A:ILE157 2.3 36.5 1.0 O1G A:ATP402 2.3 50.8 1.0 OD2 A:ASP200 2.4 38.4 1.0 CG A:ASP156 2.8 44.3 1.0 OD2 A:ASP156 2.8 50.3 1.0 HH21 A:ARG283 3.1 59.8 1.0 PB A:ATP402 3.2 49.8 1.0 H5'2 A:ATP402 3.3 67.5 1.0 PA A:ATP402 3.4 54.3 1.0 CG A:ASP200 3.4 41.6 1.0 MG A:MG404 3.4 52.0 1.0 C A:ILE157 3.4 34.8 1.0 PG A:ATP402 3.5 52.5 1.0 H A:PHE160 3.5 45.0 1.0 O3B A:ATP402 3.5 64.1 1.0 O3A A:ATP402 3.5 57.0 1.0 OD1 A:ASP200 3.6 43.2 1.0 H A:ILE157 3.6 41.2 1.0 HB3 A:PHE160 3.6 49.0 1.0 O A:HOH502 3.8 61.3 1.0 N A:ILE157 3.8 34.3 1.0 HB2 A:PHE160 3.9 49.0 1.0 NH2 A:ARG283 3.9 49.8 1.0 HB A:ILE157 4.1 37.8 1.0 C5' A:ATP402 4.1 56.2 1.0 HH22 A:ARG283 4.1 59.8 1.0 CA A:ILE157 4.1 32.6 1.0 HA A:VAL158 4.2 41.6 1.0 CB A:PHE160 4.2 40.8 1.0 CB A:ASP156 4.2 40.6 1.0 O5' A:ATP402 4.2 53.6 1.0 H A:SER159 4.2 44.7 0.8 H A:SER159 4.3 44.7 0.2 H5'1 A:ATP402 4.3 67.5 1.0 N A:PHE160 4.4 37.5 1.0 O3G A:ATP402 4.4 45.9 1.0 O1A A:ATP402 4.4 53.3 1.0 C A:ASP156 4.5 33.6 1.0 N A:VAL158 4.5 31.2 1.0 N A:SER159 4.6 37.2 1.0 HE A:ARG283 4.6 66.5 1.0 O1B A:ATP402 4.6 48.2 1.0 O2G A:ATP402 4.6 56.7 1.0 CB A:ILE157 4.6 31.4 1.0 HG A:CYS201 4.7 58.6 0.6 HB2 A:ASP156 4.7 48.8 1.0 CA A:VAL158 4.7 34.5 1.0 HB3 A:ASP156 4.7 48.8 1.0 O A:HOH513 4.7 55.9 1.0 HG22 A:ILE157 4.8 37.8 1.0 C A:VAL158 4.8 35.7 1.0 CB A:ASP200 4.8 41.1 1.0 CA A:ASP156 4.8 36.9 1.0 HA A:ASP156 4.9 44.3 1.0 HB2 A:ASP200 5.0 49.4 1.0 CA A:PHE160 5.0 39.1 1.0

Magnesium binding site 2 out of 2 in the Cryogenic Crystal Structure of the Photoactivated Adenylate Cyclase Oapac with Atp Bound


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 with Atp Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:52.0 occ:1.00 O2A A:ATP402 2.1 44.7 1.0 O A:HOH611 2.2 53.8 1.0 HG A:CYS201 2.3 58.6 0.6 OD1 A:ASP200 2.4 43.2 1.0 O A:HOH575 2.5 51.6 1.0 H5'2 A:ATP402 3.1 67.5 1.0 PA A:ATP402 3.1 54.3 1.0 SG A:CYS201 3.1 48.8 0.6 OD1 A:ASP156 3.3 57.5 1.0 O4' A:ATP402 3.3 52.3 1.0 OD2 A:ASP156 3.4 50.3 1.0 CG A:ASP200 3.4 41.6 1.0 MG A:MG403 3.4 38.0 1.0 CG A:ASP156 3.4 44.3 1.0 O1A A:ATP402 3.4 53.3 1.0 O5' A:ATP402 3.5 53.6 1.0 O A:HOH502 3.6 61.3 1.0 C5' A:ATP402 3.6 56.2 1.0 OD2 A:ASP200 3.7 38.4 1.0 H8 A:ATP402 3.8 72.8 1.0 C8 A:ATP402 3.9 60.6 1.0 H A:ASP200 4.0 46.9 1.0 HB2 A:ASP156 4.0 48.8 1.0 C4' A:ATP402 4.1 53.1 1.0 HB2 A:CYS201 4.1 50.2 0.4 N9 A:ATP402 4.1 54.2 1.0 HB3 A:CYS201 4.2 50.2 0.4 C1' A:ATP402 4.3 52.4 1.0 CB A:ASP156 4.4 40.6 1.0 N7 A:ATP402 4.5 60.0 1.0 O3A A:ATP402 4.5 57.0 1.0 H5'1 A:ATP402 4.5 67.5 1.0 CB A:CYS201 4.6 41.8 0.4 H4' A:ATP402 4.7 63.8 1.0 CB A:CYS201 4.7 41.7 0.6 O1G A:ATP402 4.7 50.8 1.0 H1' A:ATP402 4.7 63.0 1.0 N A:CYS201 4.7 39.1 1.0 O2B A:ATP402 4.7 46.1 1.0 N A:ASP200 4.7 39.0 1.0 H A:CYS201 4.7 47.1 0.6 H A:CYS201 4.7 47.1 0.4 CB A:ASP200 4.8 41.1 1.0 C4 A:ATP402 4.8 55.4 1.0 C A:ASP200 4.9 37.2 1.0 O A:ILE198 4.9 38.5 1.0 O A:HOH513 5.0 55.9 1.0 C5 A:ATP402 5.0 54.2 1.0 HB3 A:ASP156 5.0 48.8 1.0 HB3 A:CYS201 5.0 50.2 0.6

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.