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

Enzymatic activity of 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;

Protein crystallography data

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

Manganese Binding Sites:

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 2qcs

Go back to Manganese Binding Sites List in 2qcs
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 2qcs

Go back to Manganese Binding Sites List in 2qcs
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

Reference:

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
Page generated: Tue Dec 15 04:04:55 2020

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