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Potassium in PDB 6evc: Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid

Enzymatic activity of Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid

All present enzymatic activity of Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid:
4.1.1.102;

Protein crystallography data

The structure of Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid, PDB code: 6evc 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) 44.05 / 1.18
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.240, 64.330, 88.100, 90.00, 90.00, 90.00
R / Rfree (%) 14.1 / 15.8

Other elements in 6evc:

The structure of Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid also contains other interesting chemical elements:

Fluorine (F) 5 atoms
Manganese (Mn) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid (pdb code 6evc). 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 E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid, PDB code: 6evc:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6evc

Go back to Potassium Binding Sites List in 6evc
Potassium binding site 1 out of 2 in the Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:7.4
occ:1.00
OE2 A:GLU233 2.8 7.1 1.0
O A:MET225 2.8 7.6 1.0
O A:ALA222 2.8 7.3 1.0
O3P A:4LU601 2.9 6.5 1.0
O5' A:4LU601 3.0 6.8 1.0
O A:TRP169 3.1 7.0 1.0
O A:SER223 3.1 8.1 1.0
O A:HOH767 3.3 7.1 1.0
P A:4LU601 3.4 6.6 1.0
C A:SER223 3.5 7.4 1.0
CD A:GLU233 3.6 6.9 1.0
O2P A:4LU601 3.7 7.7 1.0
MN A:MN602 3.7 7.0 1.0
CA A:SER223 3.7 6.9 1.0
CG A:GLU233 3.8 7.0 1.0
C A:ALA222 3.9 6.3 1.0
C A:MET225 3.9 6.8 1.0
N A:MET225 4.1 6.8 1.0
C5' A:4LU601 4.2 6.9 1.0
N A:SER223 4.3 6.5 1.0
C A:TRP169 4.3 7.0 1.0
C4' A:4LU601 4.3 6.9 1.0
O4' A:4LU601 4.3 8.2 1.0
CB A:SER170 4.4 7.1 1.0
N A:SER224 4.4 6.5 0.5
N A:SER224 4.4 6.2 0.5
CA A:SER170 4.5 7.3 1.0
CA A:MET225 4.6 7.4 1.0
OE1 A:GLU233 4.7 7.5 1.0
C A:SER224 4.8 7.4 0.5
C A:SER224 4.8 7.6 0.5
O1P A:4LU601 4.9 7.0 1.0
ND2 A:ASN168 4.9 7.2 1.0
N A:SER170 4.9 6.3 1.0
N A:ILE227 4.9 7.2 1.0
N A:PRO226 4.9 6.5 1.0
CG1 A:ILE227 4.9 9.1 1.0
CB A:SER223 5.0 6.8 1.0
CA A:SER224 5.0 6.4 0.5

Potassium binding site 2 out of 2 in 6evc

Go back to Potassium Binding Sites List in 6evc
Potassium binding site 2 out of 2 in the Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of E282Q A. Niger FDC1 in Complex with Pentafluoro-Cinnamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K604

b:8.0
occ:1.00
O A:LEU461 2.7 9.1 1.0
O A:ARG421 2.7 7.9 1.0
O A:ASP459 2.7 7.7 1.0
O A:HOH947 2.8 13.8 1.0
O A:HOH1224 2.8 10.6 1.0
OD2 A:ASP427 2.8 8.4 1.0
CG A:ASP427 3.4 8.8 1.0
O A:HOH1039 3.5 14.9 1.0
C A:ASP459 3.8 7.1 1.0
C A:LEU461 3.8 7.5 1.0
C A:ARG421 3.9 6.9 1.0
CB A:ASP427 3.9 7.8 1.0
CA A:CYS422 4.1 6.9 1.0
OD1 A:ASP427 4.1 9.7 1.0
N A:LEU461 4.2 7.8 1.0
O A:HOH812 4.3 9.8 1.0
CA A:ALA460 4.3 7.3 1.0
C A:ALA460 4.4 6.9 1.0
N A:ALA460 4.4 6.5 1.0
N A:CYS422 4.4 6.7 1.0
CB A:ASP459 4.5 8.4 1.0
CG A:ASP459 4.5 10.2 1.0
CA A:LEU461 4.6 7.4 1.0
N A:MET462 4.6 8.3 1.0
CA A:MET462 4.7 8.5 1.0
N A:ARG423 4.7 7.0 1.0
OD1 A:ASP459 4.8 10.4 1.0
CA A:ASP459 4.8 7.4 1.0
OD2 A:ASP459 4.8 13.2 1.0
CA A:ARG421 4.9 6.8 1.0
CB A:CYS422 5.0 7.0 1.0

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: Mon Aug 12 16:03:47 2024

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