Potassium in PDB 7o5i: Crystal Structure of Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1

The structure of Crystal Structure of Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1, PDB code: 7o5i was solved by J.Laustsen, I.Justo, S.R.Marsden, U.Hanefeld, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.04 / 1.35
Space group	P 42 3 2
Cell size a, b, c (Å), α, β, γ (°)	116.376, 116.376, 116.376, 90, 90, 90
R / Rfree (%)	13.2 / 16.1

The structure of Crystal Structure of Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 also contains other interesting chemical elements:

Bromine

(Br)

2 atoms

The binding sites of Potassium atom in the Crystal Structure of Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 (pdb code 7o5i). 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 Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1, PDB code: 7o5i:

Potassium binding site 1 out of 1 in the Crystal Structure of Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1


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 Apo-Swhka (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K306 b:18.5 occ:1.00 O A:ALA31 2.6 17.1 1.0 O A:LEU33 2.7 17.4 1.0 O A:HOH612 2.7 29.2 1.0 O A:TYR35 2.8 16.6 1.0 O A:GLY63 2.9 18.9 1.0 O A:HOH548 2.9 27.4 1.0 HB2 A:ALA64 3.4 20.2 1.0 H A:TYR35 3.4 19.7 1.0 C A:GLY63 3.6 17.9 1.0 C A:ALA31 3.8 15.9 1.0 HA A:ASP34 3.9 20.6 1.0 C A:LEU33 3.9 17.6 1.0 C A:TYR35 3.9 16.1 1.0 HA A:ALA64 4.0 19.6 1.0 HA A:ARG32 4.0 19.1 1.0 N A:TYR35 4.0 16.4 1.0 HE2 A:LYS3 4.1 50.7 1.0 HZ3 A:LYS3 4.2 66.5 1.0 CB A:ALA64 4.2 16.9 1.0 N A:ALA64 4.2 16.4 1.0 HA3 A:GLY63 4.2 22.6 1.0 HZ1 A:LYS3 4.2 66.5 1.0 C A:ARG32 4.3 15.7 1.0 CA A:ALA64 4.3 16.4 1.0 HB2 A:TYR35 4.3 18.3 1.0 O A:HOH442 4.4 23.2 1.0 CA A:ARG32 4.5 15.9 1.0 O A:ARG32 4.5 17.9 1.0 HA A:ALA31 4.5 19.1 1.0 N A:LEU33 4.5 16.1 1.0 CA A:TYR35 4.5 15.9 1.0 CA A:GLY63 4.5 18.8 1.0 NZ A:LYS3 4.6 55.4 1.0 CA A:ASP34 4.6 17.1 1.0 O A:GLY62 4.6 20.6 1.0 N A:ARG32 4.6 15.6 1.0 HB1 A:ALA64 4.7 20.2 1.0 HA A:ASP36 4.7 19.4 1.0 C A:ASP34 4.7 17.7 1.0 N A:ASP34 4.7 17.3 1.0 H A:LEU33 4.8 19.4 1.0 CA A:ALA31 4.8 15.9 1.0 CE A:LYS3 4.8 42.2 1.0 H A:ALA64 4.9 19.7 1.0 HB3 A:ALA64 4.9 20.2 1.0 O A:HOH560 4.9 36.1 1.0 CA A:LEU33 4.9 16.8 1.0 CB A:TYR35 4.9 15.2 1.0

S.R.Marsden, H.J.Wijma, M.K.F.Mohr, I.Justo, P.L.Hagedoorn, J.Laustsen, C.M.Jeffries, D.Svergun, L.Mestrom, D.G.G.Mcmillan, I.Bento, U.Hanefeld. Substrate Induced Movement of the Metal Cofactor Between Active and Resting State. Angew.Chem.Int.Ed.Engl. V. 61 13338 2022.
ISSN: ESSN 1521-3773
PubMed: 36214476
DOI: 10.1002/ANIE.202213338