Potassium in PDB 6h6x: Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn

The structure of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn, PDB code: 6h6x was solved by K.A.P.Payne, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.86 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	167.720, 63.930, 98.300, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 24.8

The structure of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn also contains other interesting chemical elements:

Manganese	(Mn)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Potassium atom in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn (pdb code 6h6x). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn, PDB code: 6h6x:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn within 5.0Å range: probe atom residue distance (Å) B Occ B:K501 b:42.4 occ:1.00 OE2 B:GLU210 2.7 38.3 1.0 O B:SER200 2.7 34.7 1.0 O B:VAL148 2.7 35.8 1.0 O5' B:4LU503 2.8 46.7 1.0 O2P B:4LU503 2.8 43.4 1.0 O B:ALA202 3.0 50.3 1.0 O4' B:4LU503 3.2 48.6 1.0 P B:4LU503 3.3 46.7 1.0 CD B:GLU210 3.4 38.4 1.0 O B:HOH613 3.5 43.8 1.0 C B:SER200 3.6 37.1 1.0 O1P B:4LU503 3.7 51.1 1.0 MN B:MN502 3.7 44.4 1.0 C4' B:4LU503 3.7 46.6 1.0 CG B:GLU210 3.9 39.6 1.0 C B:VAL148 3.9 32.0 1.0 C5' B:4LU503 3.9 45.3 1.0 C B:ALA202 4.1 51.3 1.0 OE1 B:GLU210 4.3 32.8 1.0 CA B:SER149 4.3 31.9 1.0 CB B:SER149 4.3 35.5 1.0 N B:ALA202 4.3 46.0 1.0 N B:GLN201 4.4 34.7 1.0 C B:GLN201 4.4 39.2 1.0 CA B:SER200 4.5 34.7 1.0 CA B:GLN201 4.5 36.5 1.0 N B:SER149 4.5 30.4 1.0 ND2 B:ASN147 4.6 36.6 1.0 O B:HOH628 4.6 56.6 1.0 O3P B:4LU503 4.7 48.8 1.0 CA B:ALA202 4.8 51.1 1.0 CB B:GLU210 4.9 37.3 1.0 O B:ALA199 4.9 35.5 1.0 OD1 B:ASN147 4.9 37.6 1.0 O B:GLN201 4.9 48.0 1.0

Potassium binding site 2 out of 2 in the Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of An Evolved Dimeric Form of the Ubid-Class Enzyme Hmff From Pelotomaculum Thermopropionicum in Complex with Prfmn within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:51.5 occ:1.00 O5' A:4LU503 2.6 62.6 1.0 OE2 A:GLU210 2.6 47.4 1.0 O A:SER200 2.7 45.1 1.0 O2P A:4LU503 2.8 59.0 1.0 O A:VAL148 2.8 44.1 1.0 O4' A:4LU503 3.0 47.2 1.0 O A:ALA202 3.0 61.2 1.0 P A:4LU503 3.2 61.6 1.0 CD A:GLU210 3.5 46.6 1.0 O A:HOH633 3.5 49.6 1.0 C4' A:4LU503 3.7 58.3 1.0 C A:SER200 3.7 41.6 1.0 O1P A:4LU503 3.7 60.9 1.0 C5' A:4LU503 3.8 58.2 1.0 MN A:MN502 3.8 61.9 1.0 CG A:GLU210 3.9 48.6 1.0 C A:VAL148 4.0 43.6 1.0 C A:ALA202 4.2 66.3 1.0 N A:ALA202 4.4 51.0 1.0 CA A:SER149 4.4 48.0 1.0 OE1 A:GLU210 4.4 43.5 1.0 CB A:SER149 4.4 46.9 1.0 C A:GLN201 4.4 43.4 1.0 N A:GLN201 4.4 40.9 1.0 CA A:GLN201 4.5 44.9 1.0 O3P A:4LU503 4.6 50.9 1.0 CA A:SER200 4.6 39.1 1.0 ND2 A:ASN147 4.6 57.1 1.0 N A:SER149 4.6 42.9 1.0 CA A:ALA202 4.8 60.7 1.0 OD1 A:ASN147 4.8 52.3 1.0 CB A:GLU210 5.0 48.2 1.0 O A:ALA199 5.0 39.1 1.0

K.A.P.Payne, S.A.Marshall, K.Fisher, M.J.Cliff, D.M.Cannas, C.Yan, D.J.Heyes, D.A.Parker, I.Larrosa, D.Leys. Enzymatic Carboxylation of 2-Furoic Acid Yields 2,5-Furandicarboxylic Acid (Fdca). Acs Catalysis V. 9 2854 2019.
ISSN: ESSN 2155-5435
PubMed: 31057985
DOI: 10.1021/ACSCATAL.8B04862