Potassium in PDB 1h89: Crystal Structure of Ternary Protein-Dna COMPLEX2

The structure of Crystal Structure of Ternary Protein-Dna COMPLEX2, PDB code: 1h89 was solved by T.H.Tahirov, K.Ogata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.94 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.684, 73.383, 161.699, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 26.7

The binding sites of Potassium atom in the Crystal Structure of Ternary Protein-Dna COMPLEX2 (pdb code 1h89). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Ternary Protein-Dna COMPLEX2, PDB code: 1h89:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Ternary Protein-Dna COMPLEX2


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 Ternary Protein-Dna COMPLEX2 within 5.0Å range: probe atom residue distance (Å) B Occ C:K1192 b:80.0 occ:1.00 O C:LEU122 2.5 60.0 1.0 O C:ALA119 2.6 65.4 1.0 O C:ARG125 2.8 71.4 1.0 C C:ALA119 3.3 64.8 1.0 C C:LEU122 3.5 69.2 1.0 CA C:LYS120 3.8 68.6 1.0 N C:LYS120 3.9 67.6 1.0 C C:ARG125 4.0 61.7 1.0 C C:LYS120 4.1 69.0 1.0 N C:GLY124 4.2 85.4 1.0 N C:ARG125 4.2 71.2 1.0 N C:LEU122 4.2 58.5 1.0 O C:LYS120 4.3 73.9 1.0 CA C:LEU122 4.3 64.0 1.0 CB C:ALA119 4.4 58.7 1.0 N C:LYS123 4.4 79.1 1.0 CA C:ALA119 4.4 59.9 1.0 CA C:LYS123 4.5 87.6 1.0 C C:LYS123 4.6 84.9 1.0 CA C:ARG125 4.6 69.0 1.0 C C:GLY124 4.8 76.0 1.0 CB C:LEU122 4.8 48.3 1.0 N C:HIS121 4.9 65.9 1.0 CD C:LYS120 4.9 65.5 1.0 CA C:GLY124 5.0 83.7 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Ternary Protein-Dna COMPLEX2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Ternary Protein-Dna COMPLEX2 within 5.0Å range: probe atom residue distance (Å) B Occ C:K1193 b:61.9 occ:1.00 O C:LEU173 2.7 69.6 1.0 O C:ARG176 3.0 50.1 1.0 O C:ALA170 3.0 36.7 1.0 O C:PRO174 3.2 91.6 1.0 O C:HOH2018 3.4 52.4 1.0 N C:ARG176 3.7 60.2 1.0 C C:PRO174 3.8 78.8 1.0 C C:LEU173 3.9 76.1 1.0 C C:ARG176 3.9 53.6 1.0 C C:ALA170 4.0 44.1 1.0 N C:GLY175 4.4 65.5 1.0 CA C:ARG176 4.4 54.9 1.0 C C:GLY175 4.4 55.3 1.0 CA C:GLY175 4.4 56.5 1.0 CA C:PRO174 4.6 66.6 1.0 N C:PRO174 4.7 77.2 1.0 CB C:ALA170 4.8 50.0 1.0 CA C:ALA170 4.8 52.1 1.0 N C:LYS171 4.9 49.9 1.0 CA C:LEU173 4.9 75.5 1.0 CA C:LYS171 4.9 52.2 1.0 N C:THR177 5.0 46.8 1.0

T.H.Tahirov, K.Sato, E.Ichikawa-Iwata, M.Sasaki, T.Inoue-Bungo, M.Shiina, K.Kimura, S.Takata, A.Fujikawa, H.Morii, T.Kumasaka, M.Yamamoto, S.Ishii, K.Ogata. Mechanism of C-Myb-C/Ebpbeta Cooperation From Separated Sites on A Promoter Cell(Cambridge,Mass.) V. 108 57 2002.
ISSN: ISSN 0092-8674
PubMed: 11792321
DOI: 10.1016/S0092-8674(01)00636-5