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Potassium in PDB 5ytz: Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex

Protein crystallography data

The structure of Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex, PDB code: 5ytz was solved by M.H.Hou, P.C.Wu, Y.F.Kao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.16 / 1.55
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 41.759, 41.759, 138.415, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 23.5

Other elements in 5ytz:

The structure of Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex also contains other interesting chemical elements:

Manganese (Mn) 2 atoms
Bromine (Br) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex (pdb code 5ytz). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex, PDB code: 5ytz:

Potassium binding site 1 out of 1 in 5ytz

Go back to Potassium Binding Sites List in 5ytz
Potassium binding site 1 out of 1 in the Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Echinomycin-D(Acgtcgt)2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K103

b:18.0
occ:0.48
O D:MVA4 2.8 34.9 1.0
O D:N2C3 2.8 10.0 1.0
O D:HOH205 2.9 22.0 1.0
O D:HOH202 3.2 18.6 1.0
C D:MVA4 3.7 25.3 1.0
O D:HOH208 3.9 32.6 1.0
C D:N2C3 3.9 11.1 1.0
CA D:MVA4 4.1 10.7 1.0
SG D:NCY7 4.5 11.7 1.0
N D:MVA4 4.5 9.7 1.0
OG D:DSN5 4.5 10.8 1.0
O F:HOH207 4.6 33.9 1.0
CB D:N2C3 4.8 9.3 1.0
CB D:DSN5 5.0 11.1 1.0
O D:DSN5 5.0 10.4 1.0

Reference:

P.C.Wu, S.L.Tzeng, C.K.Chang, Y.F.Kao, M.J.Waring, M.H.Hou. Cooperative Recognition of T:T Mismatch By Echinomycin Causes Structural Distortions in Dna Duplex Nucleic Acids Res. V. 46 7396 2018.
ISSN: ESSN 1362-4962
PubMed: 29741655
DOI: 10.1093/NAR/GKY345
Page generated: Mon Dec 14 00:15:08 2020

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