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Sodium in PDB 4ct2: Human PDK1-Pkczeta Kinase Chimera

Enzymatic activity of Human PDK1-Pkczeta Kinase Chimera

All present enzymatic activity of Human PDK1-Pkczeta Kinase Chimera:
2.7.11.1;

Protein crystallography data

The structure of Human PDK1-Pkczeta Kinase Chimera, PDB code: 4ct2 was solved by J.O.Schulze, H.Zhang, L.A.Lopez-Garcia, R.M.Biondi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.309 / 1.25
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 147.550, 44.630, 47.610, 90.00, 100.96, 90.00
R / Rfree (%) 19.22 / 22.56

Sodium Binding Sites:

The binding sites of Sodium atom in the Human PDK1-Pkczeta Kinase Chimera (pdb code 4ct2). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Human PDK1-Pkczeta Kinase Chimera, PDB code: 4ct2:

Sodium binding site 1 out of 1 in 4ct2

Go back to Sodium Binding Sites List in 4ct2
Sodium binding site 1 out of 1 in the Human PDK1-Pkczeta Kinase Chimera


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human PDK1-Pkczeta Kinase Chimera within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na700

b:50.5
occ:1.00
O1G A:ATP500 2.3 58.2 1.0
OD2 A:ASP223 2.5 33.2 0.4
OD2 A:ASP223 2.5 33.2 0.6
O A:HOH2173 2.6 37.4 1.0
O2B A:ATP500 2.8 52.1 1.0
O A:HOH2172 3.1 38.6 1.0
O A:HOH2176 3.2 36.5 1.0
PG A:ATP500 3.4 68.3 1.0
CG A:ASP223 3.5 31.9 0.6
CG A:ASP223 3.5 31.9 0.4
O3G A:ATP500 3.6 48.8 1.0
PB A:ATP500 3.7 58.9 1.0
OD1 A:ASP223 3.8 34.0 0.4
OD1 A:ASP223 3.8 34.0 0.6
OD2 A:ASP205 3.9 21.4 1.0
O A:HOH2183 4.0 36.9 1.0
O3B A:ATP500 4.0 69.6 1.0
HD22 A:ASN210 4.0 26.1 1.0
O1B A:ATP500 4.3 54.9 1.0
HZ2 A:LYS207 4.3 28.1 1.0
O2G A:ATP500 4.8 70.1 1.0
CB A:ASP223 4.8 27.2 0.6
HE2 A:LYS207 4.8 26.5 1.0
CB A:ASP223 4.8 27.2 0.4
HB2 A:ASP223 4.8 32.7 0.6
ND2 A:ASN210 4.8 21.7 1.0
OD1 A:ASN210 4.9 21.5 1.0
HB3 A:ASP223 4.9 32.7 0.4

Reference:

H.Zhang, S.Neimanis, L.A.Lopez-Garcia, J.M.Arencibia, S.Amon, A.Stroba, S.Zeuzem, E.Proschak, H.Stark, A.F.Bauer, K.Busschots, T.J.Jorgensen, M.Engel, J.O.Schulze, R.M.Biondi. Molecular Mechanism of Regulation of the Atypical Protein Kinase C By N-Terminal Domains and An Allosteric Small Compound. Chem.Biol. V. 21 754 2014.
ISSN: ISSN 1074-5521
PubMed: 24836908
DOI: 10.1016/J.CHEMBIOL.2014.04.007
Page generated: Mon Oct 7 14:47:37 2024

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