Potassium in PDB 5d8s: 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa

All present enzymatic activity of 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa:
1.16.3.1;

The structure of 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa, PDB code: 5d8s was solved by S.Lovell, K.P.Battaile, Y.Wang, H.Yao, M.Rivera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.72 / 2.55
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	205.556, 205.556, 115.769, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 26.1

The structure of 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Iron

(Fe)

7 atoms

The binding sites of Potassium atom in the 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa (pdb code 5d8s). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa, PDB code: 5d8s:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:K201 b:24.5 occ:1.00 OE1 D:GLN151 2.9 33.5 1.0 OD1 K:ASN148 2.9 36.1 1.0 OE1 G:GLN151 2.9 27.4 1.0 OE1 A:GLN151 2.9 32.9 1.0 OD1 D:ASN148 3.0 23.4 1.0 OD1 A:ASN148 3.0 39.8 1.0 OE1 K:GLN151 3.0 30.9 1.0 OD1 G:ASN148 3.0 23.8 1.0 CG D:ASN148 3.7 29.5 1.0 CG K:ASN148 3.7 29.8 1.0 CG A:ASN148 3.7 36.5 1.0 CD A:GLN151 3.8 29.8 1.0 CG G:ASN148 3.8 25.9 1.0 CD G:GLN151 3.8 30.4 1.0 NE2 A:GLN151 3.9 26.0 1.0 CD D:GLN151 3.9 36.9 1.0 ND2 D:ASN148 3.9 27.0 1.0 ND2 A:ASN148 4.0 32.9 1.0 NE2 G:GLN151 4.0 26.4 1.0 ND2 K:ASN148 4.0 33.1 1.0 NE2 D:GLN151 4.0 27.3 1.0 CD K:GLN151 4.1 33.0 1.0 ND2 G:ASN148 4.3 31.3 1.0 NE2 K:GLN151 4.4 37.7 1.0 CB G:ASN148 4.9 24.0 1.0 CB D:ASN148 4.9 34.8 1.0 CB K:ASN148 4.9 35.2 1.0 CB A:ASN148 5.0 28.4 1.0

Potassium binding site 2 out of 3 in the 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:K201 b:30.2 occ:1.00 OD1 L:ASN148 2.8 22.1 1.0 OE1 H:GLN151 2.8 32.6 1.0 OD1 H:ASN148 2.9 30.2 1.0 OE1 B:GLN151 2.9 35.5 1.0 OE1 L:GLN151 3.0 33.6 1.0 OD1 B:ASN148 3.1 30.0 1.0 CG H:ASN148 3.6 32.6 1.0 CG B:ASN148 3.7 30.5 1.0 CD H:GLN151 3.7 33.5 1.0 CG L:ASN148 3.8 31.1 1.0 ND2 B:ASN148 3.8 35.0 1.0 ND2 H:ASN148 3.9 25.1 1.0 NE2 H:GLN151 3.9 37.0 1.0 CD L:GLN151 3.9 28.3 1.0 CD B:GLN151 3.9 35.0 1.0 NE2 L:GLN151 4.0 24.5 1.0 NE2 B:GLN151 4.2 35.0 1.0 ND2 L:ASN148 4.2 33.5 1.0 CB H:ASN148 4.7 30.9 1.0 CB B:ASN148 4.8 32.9 1.0

Potassium binding site 3 out of 3 in the 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of 2.55A Resolution Structure of Bfrb (E85A) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ C:K201 b:33.6 occ:1.00 OE1 E:GLN151 2.7 29.4 1.0 OE1 C:GLN151 2.7 28.0 1.0 OD1 E:ASN148 2.8 27.1 1.0 OD1 C:ASN148 3.0 38.4 1.0 CG C:ASN148 3.7 34.4 1.0 CD C:GLN151 3.7 38.8 1.0 CD E:GLN151 3.7 37.5 1.0 CG E:ASN148 3.8 42.2 1.0 NE2 C:GLN151 4.0 33.5 1.0 ND2 C:ASN148 4.0 38.2 1.0 NE2 E:GLN151 4.0 36.5 1.0 ND2 E:ASN148 4.3 44.1 1.0 CB C:ASN148 4.8 39.3 1.0 CB E:ASN148 4.9 42.8 1.0

Y.Wang, H.Yao, Y.Cheng, S.Lovell, K.P.Battaile, C.R.Midaugh, M.Rivera. Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots. Biochemistry V. 54 6162 2015.
ISSN: ISSN 0006-2960
PubMed: 26368531
DOI: 10.1021/ACS.BIOCHEM.5B00937