Manganese in PDB 3n0z: Adenylate Cyclase Class IV with Active Site Ligand 3AT

All present enzymatic activity of Adenylate Cyclase Class IV with Active Site Ligand 3AT:
4.6.1.1;

The structure of Adenylate Cyclase Class IV with Active Site Ligand 3AT, PDB code: 3n0z was solved by D.T.Gallagher, P.T.Reddy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.543, 37.975, 81.277, 90.00, 99.08, 90.00
R / Rfree (%)	20.6 / 25.1

The binding sites of Manganese atom in the Adenylate Cyclase Class IV with Active Site Ligand 3AT (pdb code 3n0z). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Adenylate Cyclase Class IV with Active Site Ligand 3AT, PDB code: 3n0z:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Adenylate Cyclase Class IV with Active Site Ligand 3AT


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Adenylate Cyclase Class IV with Active Site Ligand 3AT within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn182 b:30.5 occ:0.70 O2A A:3AT181 2.1 31.4 0.7 O1G A:3AT181 2.1 31.1 0.7 O2B A:3AT181 2.2 21.7 0.7 OE1 A:GLU136 2.4 34.7 1.0 OE2 A:GLU136 2.4 33.4 1.0 CD A:GLU136 2.7 29.8 1.0 OE1 A:GLU12 2.7 43.3 1.0 PB A:3AT181 3.2 26.8 0.7 PA A:3AT181 3.3 32.2 0.7 PG A:3AT181 3.4 27.9 0.7 O3A A:3AT181 3.6 28.6 0.7 O3B A:3AT181 3.6 31.2 0.7 CD A:GLU12 3.9 36.7 1.0 O2G A:3AT181 4.0 29.1 0.7 O1A A:3AT181 4.1 30.9 0.7 NH1 A:ARG113 4.1 26.1 1.0 CG A:GLU136 4.2 30.2 1.0 OE2 A:GLU12 4.3 45.0 1.0 O3G A:3AT181 4.5 32.2 0.7 O5' A:3AT181 4.5 34.1 0.7 OE1 A:GLU10 4.6 40.0 1.0 O1B A:3AT181 4.6 22.7 0.7 CE1 A:TYR173 5.0 23.7 1.0 CB A:GLU136 5.0 28.0 1.0

Manganese binding site 2 out of 2 in the Adenylate Cyclase Class IV with Active Site Ligand 3AT


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Adenylate Cyclase Class IV with Active Site Ligand 3AT within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn182 b:23.9 occ:0.80 O2B B:3AT181 2.1 23.0 0.8 O1G B:3AT181 2.2 20.9 0.8 OE2 B:GLU12 2.2 38.8 1.0 O2A B:3AT181 2.2 23.7 0.8 OE1 B:GLU136 2.2 27.1 1.0 OE2 B:GLU136 2.3 30.4 1.0 CD B:GLU136 2.6 26.9 1.0 CD B:GLU12 2.9 34.2 1.0 PB B:3AT181 3.2 21.5 0.8 PA B:3AT181 3.2 25.4 0.8 OE1 B:GLU12 3.3 41.9 1.0 PG B:3AT181 3.4 23.6 0.8 O3A B:3AT181 3.5 21.4 0.8 O3B B:3AT181 3.7 24.1 0.8 NZ B:LYS76 3.9 39.5 1.0 CG B:GLU136 4.1 25.7 1.0 O1A B:3AT181 4.1 23.9 0.8 CG B:GLU12 4.1 32.7 1.0 O2G B:3AT181 4.1 19.9 0.8 NH2 B:ARG113 4.3 24.1 1.0 NZ B:LYS14 4.3 30.6 1.0 O5' B:3AT181 4.5 27.2 0.8 O1B B:3AT181 4.5 23.1 0.8 O3G B:3AT181 4.6 23.6 0.8 CB B:GLU136 4.8 22.5 1.0 OE1 B:GLU10 4.8 48.2 1.0

D.T.Gallagher, S.K.Kim, H.Robinson, P.T.Reddy. Active-Site Structure of Class IV Adenylyl Cyclase and Transphyletic Mechanism. J.Mol.Biol. V. 405 787 2011.
ISSN: ISSN 0022-2836
PubMed: 21094652
DOI: 10.1016/J.JMB.2010.11.026