Manganese 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:

Potassium	(K)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese 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 Manganese binding site number: 1; 2;

Manganese 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 Manganese with other atoms in the Mn 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:Mn502 b:44.4 occ:1.00 OD1 B:ASN147 2.0 37.6 1.0 O2P B:4LU503 2.2 43.4 1.0 ND1 B:HIS169 2.3 40.6 1.0 OE2 B:GLU210 2.3 38.3 1.0 O B:HOH613 2.4 43.8 1.0 O B:HOH603 2.4 41.4 1.0 CG B:ASN147 3.0 39.9 1.0 CE1 B:HIS169 3.0 51.3 1.0 CD B:GLU210 3.2 38.4 1.0 P B:4LU503 3.4 46.7 1.0 CG B:HIS169 3.4 46.5 1.0 ND2 B:ASN147 3.4 36.6 1.0 OE1 B:GLU210 3.4 32.8 1.0 O1P B:4LU503 3.6 51.1 1.0 K B:K501 3.7 42.4 1.0 CB B:HIS169 3.8 40.4 1.0 O B:HOH672 4.2 55.0 1.0 NE2 B:HIS169 4.2 51.6 1.0 O3P B:4LU503 4.3 48.8 1.0 OG1 B:THR204 4.3 72.3 1.0 CB B:ASN147 4.3 35.6 1.0 CD2 B:HIS169 4.4 48.3 1.0 O5' B:4LU503 4.5 46.7 1.0 O B:VAL208 4.5 63.5 1.0 O B:ALA202 4.5 50.3 1.0 O B:VAL148 4.5 35.8 1.0 CG B:GLU210 4.6 39.6 1.0 CA B:ASN147 4.9 32.9 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn502 b:61.9 occ:1.00 OD1 A:ASN147 1.9 52.3 1.0 O2P A:4LU503 2.2 59.0 1.0 OE2 A:GLU210 2.3 47.4 1.0 ND1 A:HIS169 2.4 63.5 1.0 O A:HOH633 2.4 49.6 1.0 CG A:ASN147 3.0 55.8 1.0 CE1 A:HIS169 3.1 65.5 1.0 CD A:GLU210 3.2 46.6 1.0 OE1 A:GLU210 3.4 43.5 1.0 ND2 A:ASN147 3.5 57.1 1.0 P A:4LU503 3.5 61.6 1.0 CG A:HIS169 3.5 63.6 1.0 O1P A:4LU503 3.8 60.9 1.0 K A:K501 3.8 51.5 1.0 CB A:HIS169 4.0 58.1 1.0 OG1 A:THR204 4.2 74.3 1.0 CB A:ASN147 4.3 51.3 1.0 O A:VAL208 4.3 65.6 1.0 NE2 A:HIS169 4.3 68.8 1.0 O3P A:4LU503 4.5 50.9 1.0 CG A:GLU210 4.5 48.6 1.0 CD2 A:HIS169 4.6 68.4 1.0 O A:VAL148 4.6 44.1 1.0 O5' A:4LU503 4.6 62.6 1.0 O A:ALA202 4.7 61.2 1.0 CA A:ASN147 4.8 47.6 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