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Magnesium in PDB 4hpu: Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide

Enzymatic activity of Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide

All present enzymatic activity of Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide:
2.7.11.11;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide, PDB code: 4hpu was solved by A.C.Bastidas, J.M.Steichen, J.Wu, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.91 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.690, 79.800, 98.140, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide (pdb code 4hpu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide, PDB code: 4hpu:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4hpu

Go back to Magnesium Binding Sites List in 4hpu
Magnesium binding site 1 out of 2 in the Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg403

b:10.3
occ:1.00
O I:HOH714 1.8 16.0 1.0
O1P I:SEP21 2.0 12.1 0.5
O1B I:ANP600 2.0 11.4 0.6
O3G I:ANP600 2.1 10.0 0.6
O1B E:ANP402 2.2 8.5 0.5
O E:HOH595 2.2 13.2 1.0
OD2 E:ASP184 2.3 8.6 1.0
OD1 E:ASP184 2.3 8.2 1.0
CG E:ASP184 2.6 7.1 1.0
PG I:ANP600 3.2 10.4 0.6
PB I:ANP600 3.2 9.1 0.6
PB E:ANP402 3.4 7.6 0.5
O I:HOH747 3.4 9.8 0.5
P I:SEP21 3.4 12.2 0.5
N3B E:ANP402 3.5 9.3 0.5
N3B I:ANP600 3.5 11.0 0.6
O2G I:ANP600 3.8 8.9 0.6
O3P I:SEP21 3.8 13.3 0.5
O E:HOH739 3.8 20.6 1.0
O I:HOH731 3.9 29.1 1.0
MG E:MG404 3.9 6.7 1.0
CB E:ASP184 4.1 6.1 1.0
OD2 E:ASP166 4.2 11.6 1.0
O2B I:ANP600 4.2 11.5 0.6
NZ E:LYS72 4.3 10.3 1.0
OG I:SEP21 4.3 12.6 1.0
CA E:GLY186 4.3 7.4 1.0
O3A I:ANP600 4.4 8.6 0.6
O3A E:ANP402 4.4 7.2 0.5
O2B E:ANP402 4.5 9.3 0.5
O2P I:SEP21 4.5 11.7 0.5
O1G I:ANP600 4.5 10.9 0.6
N E:GLY186 4.5 6.5 1.0
O2A I:ANP600 4.5 8.7 0.6
O2A E:ANP402 4.6 4.8 0.5
CB I:SEP21 4.7 11.5 1.0
PA I:ANP600 4.7 9.2 0.6
O1A I:ANP600 4.8 9.3 0.6
CA E:ASP184 4.9 6.2 1.0
PA E:ANP402 4.9 5.7 0.5

Magnesium binding site 2 out of 2 in 4hpu

Go back to Magnesium Binding Sites List in 4hpu
Magnesium binding site 2 out of 2 in the Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Displaying Partial Phosphoryl Transfer of Amp-Pnp Onto A Substrate Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg404

b:6.7
occ:1.00
O2G I:ANP600 1.8 8.9 0.6
O2A I:ANP600 2.0 8.7 0.6
O2A E:ANP402 2.1 4.8 0.5
O E:HOH596 2.1 10.7 1.0
OD1 E:ASN171 2.2 7.2 1.0
OD2 E:ASP184 2.2 8.6 1.0
N3B E:ANP402 2.3 9.3 0.5
O I:HOH747 2.5 9.8 0.5
N3B I:ANP600 2.5 11.0 0.6
PG I:ANP600 2.7 10.4 0.6
CG E:ASN171 3.2 6.2 1.0
CG E:ASP184 3.2 7.1 1.0
PA I:ANP600 3.3 9.2 0.6
PA E:ANP402 3.5 5.7 0.5
PB I:ANP600 3.5 9.1 0.6
O3G I:ANP600 3.5 10.0 0.6
PB E:ANP402 3.5 7.6 0.5
ND2 E:ASN171 3.6 7.0 1.0
O1B I:ANP600 3.7 11.4 0.6
CB E:ASP184 3.7 6.1 1.0
O3A I:ANP600 3.7 8.6 0.6
O1P I:SEP21 3.8 12.1 0.5
O3A E:ANP402 3.9 7.2 0.5
O1G I:ANP600 3.9 10.9 0.6
MG E:MG403 3.9 10.3 1.0
O1B E:ANP402 3.9 8.5 0.5
CE E:LYS168 4.1 8.3 1.0
O E:HOH882 4.3 24.2 1.0
O1A I:ANP600 4.3 9.3 0.6
OD1 E:ASP184 4.3 8.2 1.0
NZ E:LYS168 4.3 8.0 1.0
O3' E:ANP402 4.3 4.4 0.5
C5' E:ANP402 4.4 4.6 0.5
O I:HOH703 4.4 13.7 1.0
O5' I:ANP600 4.4 8.4 0.6
O5' E:ANP402 4.4 4.4 0.5
OD2 E:ASP166 4.5 11.6 1.0
O1A E:ANP402 4.5 6.1 0.5
CB E:ASN171 4.6 5.8 1.0
O3' I:ANP600 4.6 11.2 0.6
C5' I:ANP600 4.6 8.5 0.6
O2P I:SEP21 4.7 11.7 0.5
O I:HOH702 4.7 22.8 1.0
O2B E:ANP402 4.8 9.3 0.5
O E:HOH595 4.8 13.2 1.0
O2B I:ANP600 4.9 11.5 0.6
P I:SEP21 4.9 12.2 0.5
C3' E:ANP402 4.9 4.2 0.5
CA E:ASN171 4.9 6.2 1.0
O E:GLU170 5.0 7.5 1.0

Reference:

A.C.Bastidas, M.S.Deal, J.M.Steichen, Y.Guo, J.Wu, S.S.Taylor. Phosphoryl Transfer By Protein Kinase A Is Captured in A Crystal Lattice. J.Am.Chem.Soc. V. 135 4788 2013.
ISSN: ISSN 0002-7863
PubMed: 23458248
DOI: 10.1021/JA312237Q
Page generated: Fri Aug 16 16:22:23 2024

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