Atomistry » Potassium » PDB 6dxz-6f3n » 6ev5
Atomistry »
  Potassium »
    PDB 6dxz-6f3n »
      6ev5 »

Potassium in PDB 6ev5: Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form

Enzymatic activity of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form

All present enzymatic activity of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form:
4.1.1.102;

Protein crystallography data

The structure of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6ev5 was solved by S.S.Bailey, D.Leys, K.A.P.Payne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.30 / 1.28
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.020, 63.510, 87.620, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19

Other elements in 6ev5:

The structure of Crystal Structure of E282Q 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 Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form (pdb code 6ev5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6ev5:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6ev5

Go back to Potassium Binding Sites List in 6ev5
Potassium binding site 1 out of 2 in the Crystal Structure of E282Q 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 Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K602

b:11.0
occ:1.00
O A:MET225 2.8 10.6 1.0
OE2 A:GLU233 2.8 10.0 1.0
O A:ALA222 2.8 11.2 1.0
O8 A:BYN604 2.9 8.6 1.0
O7 A:BYN604 3.0 9.4 1.0
O A:TRP169 3.1 9.4 1.0
O A:SER223 3.1 11.2 1.0
O A:HOH752 3.3 8.6 1.0
P1 A:BYN604 3.4 8.7 1.0
C A:SER223 3.5 10.2 1.0
CD A:GLU233 3.6 9.7 1.0
O9 A:BYN604 3.6 10.4 1.0
MN A:MN601 3.7 9.9 1.0
CA A:SER223 3.7 9.9 1.0
CG A:GLU233 3.8 10.9 1.0
C A:ALA222 3.9 10.3 1.0
C A:MET225 3.9 10.3 1.0
N A:MET225 4.1 9.6 1.0
C22 A:BYN604 4.2 9.5 1.0
C A:TRP169 4.2 8.6 1.0
C21 A:BYN604 4.3 10.4 1.0
N A:SER223 4.3 8.6 1.0
O6 A:BYN604 4.3 11.2 1.0
N A:SER224 4.3 8.9 0.5
N A:SER224 4.4 9.1 0.5
CB A:SER170 4.4 9.7 1.0
CA A:SER170 4.4 9.3 1.0
CA A:MET225 4.6 10.5 1.0
OE1 A:GLU233 4.7 11.0 1.0
C A:SER224 4.7 10.1 0.5
C A:SER224 4.8 9.8 0.5
ND2 A:ASN168 4.8 10.2 1.0
O10 A:BYN604 4.9 10.7 1.0
N A:SER170 4.9 8.4 1.0
CA A:SER224 4.9 9.5 0.5
N A:PRO226 4.9 10.2 1.0
CG1 A:ILE227 4.9 12.9 1.0
N A:ILE227 4.9 10.2 1.0
CB A:SER223 4.9 9.5 1.0

Potassium binding site 2 out of 2 in 6ev5

Go back to Potassium Binding Sites List in 6ev5
Potassium binding site 2 out of 2 in the Crystal Structure of E282Q 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 2 of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:11.4
occ:1.00
O A:ARG421 2.6 10.8 1.0
O A:ASP459 2.6 10.5 1.0
O A:LEU461 2.7 13.1 1.0
O A:HOH1015 2.8 19.0 1.0
O A:HOH1148 2.8 14.4 1.0
OD2 A:ASP427 2.8 11.7 1.0
CG A:ASP427 3.4 13.8 1.0
O A:HOH935 3.4 20.6 1.0
C A:ASP459 3.7 11.2 1.0
C A:LEU461 3.7 10.8 1.0
C A:ARG421 3.8 9.7 1.0
CB A:ASP427 3.9 11.7 1.0
N A:LEU461 4.2 11.2 1.0
OD1 A:ASP427 4.2 14.0 1.0
CA A:CYS422 4.2 9.0 1.0
O A:HOH800 4.3 12.7 1.0
CA A:ALA460 4.3 10.2 1.0
C A:ALA460 4.4 10.5 1.0
N A:ALA460 4.4 9.7 1.0
N A:CYS422 4.4 9.3 1.0
CG A:ASP459 4.5 15.0 1.0
CB A:ASP459 4.5 11.2 1.0
N A:MET462 4.6 11.1 1.0
CA A:LEU461 4.6 10.9 1.0
CA A:MET462 4.7 11.2 1.0
N A:ARG423 4.7 8.9 1.0
OD1 A:ASP459 4.7 14.7 1.0
CA A:ASP459 4.8 11.2 1.0
OD2 A:ASP459 4.8 19.8 1.0
CA A:ARG421 4.9 9.3 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 16:02:11 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy