Manganese in PDB 2qcs: A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State

All present enzymatic activity of A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State:
2.7.11.11;

The structure of A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State, PDB code: 2qcs was solved by C.Kim, C.Y.Cheng, A.S.Saldanha, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	125.809, 125.809, 140.941, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 22.5

The binding sites of Manganese atom in the A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State (pdb code 2qcs). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State, PDB code: 2qcs:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:31.7 occ:1.00 O2A A:ANP400 2.1 29.9 1.0 O A:HOH555 2.2 30.1 1.0 OD1 A:ASN171 2.2 31.2 1.0 O2G A:ANP400 2.2 25.9 1.0 OD2 A:ASP184 2.3 29.6 1.0 N3B A:ANP400 2.6 30.3 1.0 PG A:ANP400 3.0 28.6 1.0 CG A:ASN171 3.2 29.3 1.0 CG A:ASP184 3.2 32.8 1.0 PA A:ANP400 3.4 30.6 1.0 ND2 A:ASN171 3.6 27.0 1.0 CB A:ASP184 3.6 31.8 1.0 PB A:ANP400 3.8 26.9 1.0 O1G A:ANP400 3.8 33.1 1.0 O3A A:ANP400 3.8 30.2 1.0 O2B A:ANP400 3.9 28.7 1.0 MN A:MN402 4.0 28.4 1.0 CE A:LYS168 4.1 27.6 1.0 O3G A:ANP400 4.1 26.2 1.0 NZ A:LYS168 4.2 24.5 1.0 O3' A:ANP400 4.3 29.8 1.0 OD1 A:ASP184 4.3 31.2 1.0 OD2 A:ASP166 4.4 33.2 1.0 O B:HOH450 4.4 41.2 1.0 O1A A:ANP400 4.5 30.4 1.0 O5' A:ANP400 4.5 30.9 1.0 CB A:ASN171 4.5 30.5 1.0 O A:HOH550 4.6 39.8 1.0 C5' A:ANP400 4.6 29.2 1.0 C3' A:ANP400 4.8 31.1 1.0 O A:GLU170 4.8 29.8 1.0 CA A:ASN171 4.9 29.4 1.0 O A:HOH527 4.9 22.2 1.0

Manganese binding site 2 out of 2 in the A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of A Complex Structure Between the Catalytic and Regulatory Subunit of Protein Kinase A That Represents the Inhibited State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:28.4 occ:1.00 O A:HOH564 2.0 24.5 1.0 O2B A:ANP400 2.1 28.7 1.0 O1G A:ANP400 2.1 33.1 1.0 O A:HOH527 2.2 22.2 1.0 OD2 A:ASP184 2.3 29.6 1.0 OD1 A:ASP184 2.4 31.2 1.0 CG A:ASP184 2.7 32.8 1.0 PG A:ANP400 3.2 28.6 1.0 PB A:ANP400 3.3 26.9 1.0 N3B A:ANP400 3.5 30.3 1.0 O2G A:ANP400 3.7 25.9 1.0 CD1 A:PHE54 4.0 42.5 1.0 OD2 A:ASP166 4.0 33.2 1.0 MN A:MN401 4.0 31.7 1.0 CB A:ASP184 4.2 31.8 1.0 NZ A:LYS72 4.3 37.4 1.0 O A:HOH425 4.3 26.1 1.0 O1B A:ANP400 4.3 26.3 1.0 CA A:GLY186 4.4 30.6 1.0 O3A A:ANP400 4.4 30.2 1.0 CE1 A:PHE54 4.5 42.2 1.0 CB B:ALA97 4.6 30.5 1.0 O3G A:ANP400 4.6 26.2 1.0 O2A A:ANP400 4.6 29.9 1.0 N A:GLY186 4.7 30.1 1.0 O A:HOH444 4.8 29.9 1.0 CZ A:PHE187 4.9 31.3 1.0 PA A:ANP400 4.9 30.6 1.0 CG A:PHE54 5.0 42.3 1.0 O1A A:ANP400 5.0 30.4 1.0

C.Kim, C.Y.Cheng, S.A.Saldanha, S.S.Taylor. Pka-I Holoenzyme Structure Reveals A Mechanism For Camp-Dependent Activation. Cell(Cambridge,Mass.) V. 130 1032 2007.
ISSN: ISSN 0092-8674
PubMed: 17889648
DOI: 10.1016/J.CELL.2007.07.018