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Potassium in PDB 6evd: Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form

Enzymatic activity of Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form

All present enzymatic activity of Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form:
4.1.1.102;

Protein crystallography data

The structure of Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6evd was solved by S.S.Bailey, L.David, K.A.P.Payne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.85 / 1.19
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.230, 64.110, 87.440, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 16.2

Other elements in 6evd:

The structure of Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form (pdb code 6evd). 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 Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6evd:

Potassium binding site 1 out of 1 in 6evd

Go back to Potassium Binding Sites List in 6evd
Potassium binding site 1 out of 1 in the Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K602

b:7.0
occ:1.00
 OE2 A:GLU233 2.8 7.0 1.0
O A:MET225 2.8 7.2 1.0
O A:ALA222 2.8 7.2 1.0
O8 A:BYN603 2.8 6.2 1.0
O7 A:BYN603 3.0 6.8 1.0
O A:TRP169 3.1 6.5 1.0
O A:SER223 3.1 8.2 1.0
O A:HOH756 3.3 7.0 1.0
P1 A:BYN603 3.4 6.2 1.0
C A:SER223 3.5 6.6 1.0
O9 A:BYN603 3.6 6.9 1.0
CD A:GLU233 3.6 6.5 1.0
MN A:MN601 3.7 6.5 1.0
CA A:SER223 3.7 6.3 1.0
CG A:GLU233 3.8 7.1 1.0
C A:ALA222 3.9 6.2 1.0
C A:MET225 3.9 6.6 1.0
N A:MET225 4.1 7.0 1.0
C22 A:BYN603 4.2 7.3 1.0
N A:SER223 4.3 6.2 1.0
C21 A:BYN603 4.3 6.8 1.0
O6 A:BYN603 4.3 7.9 1.0
C A:TRP169 4.3 6.1 1.0
N A:SER224 4.3 6.2 0.5
N A:SER224 4.3 6.3 0.5
CB A:SER170 4.4 6.7 1.0
CA A:SER170 4.5 6.3 1.0
CA A:MET225 4.6 7.2 1.0
OE1 A:GLU233 4.7 6.8 1.0
C A:SER224 4.8 7.2 0.5
C A:SER224 4.8 6.9 0.5
O10 A:BYN603 4.8 6.7 1.0
ND2 A:ASN168 4.8 6.6 1.0
CG1 A:ILE227 4.9 8.8 1.0
N A:SER170 4.9 6.2 1.0
N A:PRO226 4.9 6.6 1.0
N A:ILE227 4.9 6.8 1.0
CA A:SER224 5.0 6.4 0.5
CB A:SER223 5.0 6.7 1.0
CA A:SER224 5.0 6.2 0.5

Reference:

S.S.Bailey, K.A.P.Payne, K.Fisher, S.A.Marshall, M.J.Cliff, R.Spiess, D.A.Parker, S.E.J.Rigby, D.Leys. The Role of Conserved Residues in Fdc Decarboxylase in Prenylated Flavin Mononucleotide Oxidative Maturation, Cofactor Isomerization, and Catalysis. J. Biol. Chem. V. 293 2272 2018.
ISSN: ESSN 1083-351X
PubMed: 29259125
DOI: 10.1074/JBC.RA117.000881
Page generated: Sat Aug 9 10:56:30 2025

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