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Manganese in PDB 3n10: Product Complex of Adenylate Cyclase Class IV

Enzymatic activity of Product Complex of Adenylate Cyclase Class IV

All present enzymatic activity of Product Complex of Adenylate Cyclase Class IV:
4.6.1.1;

Protein crystallography data

The structure of Product Complex of Adenylate Cyclase Class IV, PDB code: 3n10 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 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.477, 38.124, 80.658, 90.00, 98.71, 90.00
R / Rfree (%) 21.8 / 25.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Product Complex of Adenylate Cyclase Class IV (pdb code 3n10). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Product Complex of Adenylate Cyclase Class IV, PDB code: 3n10:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 3n10

Go back to Manganese Binding Sites List in 3n10
Manganese binding site 1 out of 3 in the Product Complex of Adenylate Cyclase Class IV


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Product Complex of Adenylate Cyclase Class IV within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn182

b:35.4
occ:1.00
OE1 A:GLU136 2.3 36.3 1.0
OE1 A:GLU10 2.3 35.4 1.0
O2P A:CMP181 2.3 42.6 1.0
OE2 A:GLU12 3.1 45.5 1.0
CD A:GLU136 3.3 29.6 1.0
CD A:GLU10 3.3 30.6 1.0
OE2 A:GLU136 3.5 39.5 1.0
OE1 A:GLU12 3.6 48.4 1.0
CD A:GLU12 3.6 35.6 1.0
P A:CMP181 3.6 43.8 1.0
OE2 A:GLU10 3.6 34.7 1.0
O3' A:CMP181 3.8 42.7 1.0
O3 A:SO4185 4.1 33.5 1.0
MN A:MN183 4.2 39.4 1.0
NZ A:LYS76 4.2 39.9 1.0
O1P A:CMP181 4.3 39.5 1.0
CG A:GLU10 4.6 29.0 1.0
CG A:GLU136 4.6 25.8 1.0
O A:HOH369 4.7 39.7 1.0
CG A:GLU12 4.8 32.4 1.0
O2 A:SO4185 4.8 39.1 1.0
O5' A:CMP181 4.8 42.7 1.0
CB A:GLU12 5.0 25.2 1.0

Manganese binding site 2 out of 3 in 3n10

Go back to Manganese Binding Sites List in 3n10
Manganese binding site 2 out of 3 in the Product Complex of Adenylate Cyclase Class IV


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Product Complex of Adenylate Cyclase Class IV within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn183

b:39.4
occ:1.00
OE2 A:GLU10 2.1 34.7 1.0
O2' A:CMP181 2.3 47.5 1.0
O3' A:CMP181 2.5 42.7 1.0
O A:HOH369 2.5 39.7 1.0
NE2 A:HIS122 2.7 28.5 1.0
C2' A:CMP181 2.7 46.0 1.0
C3' A:CMP181 3.0 44.3 1.0
CD A:GLU10 3.2 30.6 1.0
CD2 A:HIS122 3.5 28.8 1.0
CE1 A:HIS122 3.7 29.9 1.0
OE1 A:GLU10 3.8 35.4 1.0
O A:HOH372 3.8 38.1 1.0
P A:CMP181 3.9 43.8 1.0
CE2 A:PHE5 4.0 39.4 1.0
MN A:MN182 4.2 35.4 1.0
C4' A:CMP181 4.2 43.1 1.0
C1' A:CMP181 4.3 47.3 1.0
CD2 A:PHE5 4.3 38.6 1.0
O2P A:CMP181 4.3 42.6 1.0
CG A:GLU10 4.4 29.0 1.0
O1P A:CMP181 4.6 39.5 1.0
CG A:HIS122 4.7 27.5 1.0
N3 A:CMP181 4.7 48.1 1.0
ND1 A:HIS122 4.8 28.4 1.0
OG1 A:THR124 4.8 23.8 1.0
O A:HOH362 4.8 25.9 1.0
O4' A:CMP181 4.9 44.4 1.0
OE1 A:GLU136 5.0 36.3 1.0

Manganese binding site 3 out of 3 in 3n10

Go back to Manganese Binding Sites List in 3n10
Manganese binding site 3 out of 3 in the Product Complex of Adenylate Cyclase Class IV


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Product Complex of Adenylate Cyclase Class IV within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn183

b:42.9
occ:0.80
OE1 B:GLU10 2.1 41.5 1.0
O3' B:CMP181 2.4 51.9 0.8
O2' B:CMP181 2.5 47.7 0.8
NE2 B:HIS122 2.6 31.8 1.0
C2' B:CMP181 3.1 50.3 0.8
C3' B:CMP181 3.1 51.3 0.8
CD B:GLU10 3.1 38.2 1.0
CD2 B:HIS122 3.4 31.7 1.0
OE2 B:GLU10 3.5 39.8 1.0
CE1 B:HIS122 3.6 31.6 1.0
P B:CMP181 3.8 53.6 0.8
O2P B:CMP181 4.0 53.2 0.8
CB B:ALA138 4.2 22.5 1.0
C4' B:CMP181 4.3 51.8 0.8
CG B:GLU10 4.4 29.6 1.0
C1' B:CMP181 4.5 49.7 0.8
O1P B:CMP181 4.6 49.8 0.8
CG B:HIS122 4.6 27.8 1.0
CE2 B:PHE5 4.6 34.6 1.0
ND1 B:HIS122 4.7 28.5 1.0
O5' B:CMP181 4.9 52.5 0.8
OE2 B:GLU12 5.0 40.3 1.0
CD2 B:PHE5 5.0 33.1 1.0

Reference:

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
Page generated: Tue Dec 15 04:12:46 2020

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