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Magnesium in PDB 5mbk: Structure of A Bacterial Light-Regulated Adenylyl Cylcase

Protein crystallography data

The structure of Structure of A Bacterial Light-Regulated Adenylyl Cylcase, PDB code: 5mbk was solved by R.Lindner, E.Hartmann, M.Tarnawski, A.Winkler, D.Frey, J.Reinstein, A.Meinhart, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.88 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 69.600, 143.360, 57.480, 90.00, 135.91, 90.00
R / Rfree (%) 20.9 / 26.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Bacterial Light-Regulated Adenylyl Cylcase (pdb code 5mbk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of A Bacterial Light-Regulated Adenylyl Cylcase, PDB code: 5mbk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5mbk

Go back to Magnesium Binding Sites List in 5mbk
Magnesium binding site 1 out of 2 in the Structure of A Bacterial Light-Regulated Adenylyl Cylcase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Bacterial Light-Regulated Adenylyl Cylcase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:41.9
occ:1.00
O3G A:ATP401 1.9 42.8 1.0
O1B A:ATP401 2.1 45.4 1.0
OD1 A:ASP157 2.1 44.1 1.0
O2A A:ATP401 2.2 53.9 1.0
O A:ILE158 2.2 43.8 1.0
OD2 A:ASP201 2.2 42.2 1.0
NH2 A:ARG284 3.2 44.1 1.0
CG A:ASP157 3.2 40.5 1.0
PB A:ATP401 3.3 49.6 1.0
C A:ILE158 3.3 40.4 1.0
PG A:ATP401 3.3 48.2 1.0
CG A:ASP201 3.3 44.4 1.0
PA A:ATP401 3.4 55.4 1.0
MG A:MG403 3.5 47.4 1.0
N A:ILE158 3.7 33.3 1.0
O3A A:ATP401 3.7 57.5 1.0
OD2 A:ASP157 3.7 49.6 1.0
O3B A:ATP401 3.7 51.9 1.0
OD1 A:ASP201 3.8 41.5 1.0
CA A:ILE158 4.0 31.9 1.0
O2G A:ATP401 4.0 38.8 1.0
O A:HOH514 4.3 44.1 1.0
C A:ASP157 4.3 40.9 1.0
N A:LEU159 4.4 49.2 1.0
C5' A:ATP401 4.4 57.3 1.0
O1G A:ATP401 4.4 45.6 1.0
O5' A:ATP401 4.4 47.8 1.0
CZ A:ARG284 4.4 49.3 1.0
CB A:ASP157 4.4 43.3 1.0
CB A:PHE161 4.4 38.6 1.0
N A:PHE161 4.4 37.8 1.0
N A:ALA160 4.4 37.6 1.0
O1A A:ATP401 4.5 57.8 1.0
O2B A:ATP401 4.6 45.3 1.0
CB A:ILE158 4.6 33.8 1.0
CA A:LEU159 4.6 40.7 1.0
CB A:ASP201 4.7 32.9 1.0
C A:LEU159 4.8 40.3 1.0
CA A:ASP157 4.8 39.9 1.0
O A:ASP157 4.8 43.8 1.0
NE A:ARG284 4.9 51.6 1.0

Magnesium binding site 2 out of 2 in 5mbk

Go back to Magnesium Binding Sites List in 5mbk
Magnesium binding site 2 out of 2 in the Structure of A Bacterial Light-Regulated Adenylyl Cylcase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of A Bacterial Light-Regulated Adenylyl Cylcase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:47.4
occ:1.00
O A:HOH514 2.0 44.1 1.0
O2A A:ATP401 2.3 53.9 1.0
OD1 A:ASP201 2.3 41.5 1.0
OD2 A:ASP157 2.4 49.6 1.0
CG A:ASP201 3.2 44.4 1.0
CG A:ASP157 3.2 40.5 1.0
PA A:ATP401 3.2 55.4 1.0
OD2 A:ASP201 3.4 42.2 1.0
OD1 A:ASP157 3.4 44.1 1.0
MG A:MG402 3.5 41.9 1.0
O1A A:ATP401 3.6 57.8 1.0
O5' A:ATP401 3.7 47.8 1.0
C5' A:ATP401 4.0 57.3 1.0
O A:HOH542 4.2 65.2 1.0
CB A:CYS202 4.3 52.4 1.0
O4' A:ATP401 4.5 63.1 1.0
CB A:ASP157 4.5 43.3 1.0
O3G A:ATP401 4.5 42.8 1.0
N A:ASP201 4.6 47.1 1.0
CB A:ASP201 4.6 32.9 1.0
O A:ILE199 4.7 50.3 1.0
O3A A:ATP401 4.7 57.5 1.0
O1B A:ATP401 4.8 45.4 1.0
C A:ASP201 4.8 47.8 1.0
C8 A:ATP401 4.9 50.3 1.0
CA A:ASP201 4.9 45.1 1.0
C4' A:ATP401 5.0 62.6 1.0

Reference:

R.Lindner, E.Hartmann, M.Tarnawski, A.Winkler, D.Frey, J.Reinstein, A.Meinhart, I.Schlichting. Photoactivation Mechanism of A Bacterial Light-Regulated Adenylyl Cyclase. J. Mol. Biol. V. 429 1336 2017.
ISSN: ESSN 1089-8638
PubMed: 28336405
DOI: 10.1016/J.JMB.2017.03.020
Page generated: Mon Dec 14 20:51:02 2020

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