Potassium in PDB 4dk9: Crystal Structure of MBD4 Catalytic Domain Bound to Abasic Dna

The structure of Crystal Structure of MBD4 Catalytic Domain Bound to Abasic Dna, PDB code: 4dk9 was solved by B.A.Manvilla, E.A.Toth, A.C.Drohat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.10 / 2.76
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.999, 55.161, 122.193, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 25.9

The binding sites of Potassium atom in the Crystal Structure of MBD4 Catalytic Domain Bound to Abasic Dna (pdb code 4dk9). 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 MBD4 Catalytic Domain Bound to Abasic Dna, PDB code: 4dk9:

Potassium binding site 1 out of 1 in the Crystal Structure of MBD4 Catalytic Domain Bound to Abasic Dna


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 MBD4 Catalytic Domain Bound to Abasic Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:K601 b:0.6 occ:1.00 O A:LEU534 2.6 87.4 1.0 O A:ILE537 2.6 83.4 1.0 O A:ILE532 2.7 90.3 1.0 OP1 C:DC21 2.8 93.3 1.0 OP2 C:DC21 3.6 97.5 1.0 P C:DC21 3.6 94.8 1.0 C A:LEU534 3.7 87.9 1.0 C A:ILE537 3.8 80.9 1.0 C A:ILE532 3.9 86.7 1.0 N A:ILE537 4.0 83.0 1.0 N A:LEU534 4.3 87.8 1.0 N A:GLY536 4.4 89.3 1.0 CA A:ILE537 4.4 79.6 1.0 C A:GLU533 4.5 91.2 1.0 O3' C:DT20 4.5 91.9 1.0 CA A:HIS535 4.6 90.7 1.0 CA A:LEU534 4.6 87.2 1.0 N A:HIS535 4.6 89.2 1.0 CA A:ILE532 4.6 83.8 1.0 O A:GLU533 4.8 96.8 1.0 C A:HIS535 4.8 89.8 1.0 N A:GLY538 4.8 79.6 1.0 O A:PRO531 4.8 85.2 1.0 CB A:ILE537 4.9 78.0 1.0 N A:GLU533 4.9 86.7 1.0 O5' C:DC21 4.9 99.4 1.0 CA A:GLU533 5.0 89.8 1.0 CG1 A:ILE532 5.0 86.0 1.0

B.A.Manvilla, A.Maiti, M.C.Begley, E.A.Toth, A.C.Drohat. Crystal Structure of Human Methyl-Binding Domain IV Glycosylase Bound to Abasic Dna. J.Mol.Biol. V. 420 164 2012.
ISSN: ISSN 0022-2836
PubMed: 22560993
DOI: 10.1016/J.JMB.2012.04.028