Potassium in PDB 6rwv: Structure of Apo-Lmcpfc

All present enzymatic activity of Structure of Apo-Lmcpfc:
4.99.1.1;

The structure of Structure of Apo-Lmcpfc, PDB code: 6rwv was solved by S.Hofbauer, J.Helm, K.Djinovic-Carugo, P.G.Furtmueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.09 / 1.64
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.303, 76.723, 52.258, 90.00, 106.56, 90.00
R / Rfree (%)	17.6 / 20.1

The binding sites of Potassium atom in the Structure of Apo-Lmcpfc (pdb code 6rwv). 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 Apo-Lmcpfc, PDB code: 6rwv:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of Apo-Lmcpfc


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Apo-Lmcpfc within 5.0Å range: probe atom residue distance (Å) B Occ A:K410 b:63.8 occ:1.00 OE1 A:GLU186 2.7 55.3 1.0 N A:GLY231 3.0 16.9 1.0 O A:GLY231 3.2 19.6 1.0 OE2 A:GLU186 3.4 51.2 1.0 CD A:GLU186 3.4 50.0 1.0 CA A:GLY231 3.8 19.9 1.0 CA A:LEU230 3.8 17.0 1.0 C A:LEU230 3.9 17.6 1.0 C A:GLY231 3.9 22.6 1.0 CD2 A:LEU230 4.4 21.3 1.0 O A:TRP229 4.4 19.5 1.0 CB A:LEU230 4.6 15.7 1.0 CG A:GLU186 4.8 39.5 1.0 N A:LEU230 4.9 16.6 1.0 CE A:LYS189 4.9 49.5 1.0

Potassium binding site 2 out of 2 in the Structure of Apo-Lmcpfc


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Apo-Lmcpfc within 5.0Å range: probe atom residue distance (Å) B Occ A:K411 b:0.2 occ:1.00 OE1 A:GLU122 3.2 49.0 1.0 ND2 A:ASN144 3.8 29.9 1.0 CD A:GLU122 4.0 46.1 1.0 OE2 A:GLU122 4.0 50.2 1.0 OD1 A:ASN144 4.3 23.6 1.0 OH A:TYR116 4.4 28.7 1.0 CG A:ASN144 4.5 22.4 1.0 ND2 A:ASN125 4.7 19.6 1.0

S.Hofbauer, J.Helm, C.Obinger, K.Djinovic-Carugo, P.G.Furtmuller. Crystal Structures and Calorimetry Reveal Catalytically Relevant Binding Mode of Coproporphyrin and Coproheme in Coproporphyrin Ferrochelatase. Febs J. 2019.
ISSN: ISSN 1742-464X
PubMed: 31794133
DOI: 10.1111/FEBS.15164