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Magnesium in PDB 6ko6: Crystal Structure of Amppnp Bound CKA1 From C. Neoformans

Protein crystallography data

The structure of Crystal Structure of Amppnp Bound CKA1 From C. Neoformans, PDB code: 6ko6 was solved by H.S.Cho, Y.Yoo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.67 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.020, 95.800, 93.330, 90.00, 90.00, 90.00
R / Rfree (%) 23.8 / 26.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Amppnp Bound CKA1 From C. Neoformans (pdb code 6ko6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Amppnp Bound CKA1 From C. Neoformans, PDB code: 6ko6:

Magnesium binding site 1 out of 1 in 6ko6

Go back to Magnesium Binding Sites List in 6ko6
Magnesium binding site 1 out of 1 in the Crystal Structure of Amppnp Bound CKA1 From C. Neoformans


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 Amppnp Bound CKA1 From C. Neoformans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:57.6
occ:1.00
O2B B:ANP401 2.4 66.2 1.0
OD1 B:ASP174 2.5 42.0 1.0
OD2 B:ASP174 2.8 49.5 1.0
O3G B:ANP401 2.9 67.7 1.0
CG B:ASP174 3.0 44.4 1.0
PB B:ANP401 3.8 75.6 1.0
PG B:ANP401 4.0 76.7 1.0
CA B:GLY176 4.2 41.8 1.0
NZ B:LYS67 4.2 50.8 1.0
O1G B:ANP401 4.2 66.6 1.0
N3B B:ANP401 4.3 76.8 1.0
N B:GLY176 4.4 39.2 1.0
O1B B:ANP401 4.5 72.4 1.0
C B:GLY176 4.5 44.0 1.0
CB B:ASP174 4.5 43.5 1.0
N B:LEU177 4.7 44.2 1.0
OD2 B:ASP155 4.7 48.4 1.0
CG B:LEU177 4.9 44.8 1.0
O3A B:ANP401 4.9 71.8 1.0

Reference:

B.X.Ong, Y.Yoo, M.G.Han, J.B.Park, M.K.Choi, Y.Choi, J.S.Shin, Y.S.Bahn, H.S.Cho. Structural Analysis of Fungal Pathogenicity-Related Casein Kinase Alpha Subunit, CKA1, in the Human Fungal Pathogen Cryptococcus Neoformans. Sci Rep V. 9 14398 2019.
ISSN: ESSN 2045-2322
PubMed: 31591414
DOI: 10.1038/S41598-019-50678-Z
Page generated: Tue Oct 1 07:18:37 2024

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