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Potassium in PDB 4toh: 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa

Enzymatic activity of 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa

All present enzymatic activity of 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa:
1.16.3.1;

Protein crystallography data

The structure of 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa, PDB code: 4toh was solved by S.Lovell, K.P.Battaile, H.Yao, R.Kumar, K.Eshelman, M.Rivera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.23 / 1.80
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 153.993, 153.993, 155.200, 90.00, 90.00, 120.00
R / Rfree (%) 14.7 / 17.2

Other elements in 4toh:

The structure of 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Iron (Fe) 41 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa (pdb code 4toh). 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 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa, PDB code: 4toh:

Potassium binding site 1 out of 1 in 4toh

Go back to Potassium Binding Sites List in 4toh
Potassium binding site 1 out of 1 in the 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) 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 1.80A Resolution Structure of Iron Bound Bfrb (C89S, K96C) From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K201

b:19.5
occ:1.00
 OE1 B:GLN151 2.9 18.0 1.0
OE1 D:GLN151 2.9 18.7 1.0
OE1 C:GLN151 2.9 20.5 1.0
OD1 B:ASN148 2.9 20.7 1.0
OD1 C:ASN148 3.0 19.6 1.0
OD1 D:ASN148 3.0 19.4 1.0
CG B:ASN148 3.7 21.1 1.0
CG C:ASN148 3.7 23.7 1.0
CG D:ASN148 3.8 24.0 1.0
CD D:GLN151 3.8 21.9 1.0
CD B:GLN151 3.8 20.5 1.0
CD C:GLN151 3.9 24.1 1.0
NE2 D:GLN151 4.0 19.4 1.0
NE2 B:GLN151 4.0 22.8 1.0
ND2 B:ASN148 4.1 20.8 1.0
ND2 C:ASN148 4.1 22.6 1.0
ND2 D:ASN148 4.1 21.4 1.0
NE2 C:GLN151 4.1 19.7 1.0
CB B:ASN148 4.9 19.7 1.0
CB C:ASN148 4.9 20.0 1.0
CB D:ASN148 4.9 17.6 1.0

Reference:

H.Yao, H.Rui, R.Kumar, K.Eshelman, S.Lovell, K.P.Battaile, W.Im, M.Rivera. Concerted Motions Networking Pores and Distant Ferroxidase Centers Enable Bacterioferritin Function and Iron Traffic. Biochemistry 2015.
ISSN: ISSN 0006-2960
PubMed: 25640193
DOI: 10.1021/BI501255R
Page generated: Sat Aug 9 07:56:03 2025

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