Atomistry » Manganese » PDB 6e4q-6f4p » 6evd
Atomistry »
  Manganese »
    PDB 6e4q-6f4p »
      6evd »

Manganese 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:

Potassium (K) 1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total only one binding site of Manganese was determined in the Structure of R173A A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6evd:

Manganese binding site 1 out of 1 in 6evd

Go back to Manganese Binding Sites List in 6evd
Manganese 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 Manganese with other atoms in the Mn 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:Mn601

b:6.5
occ:1.00
 OE2 A:GLU233 2.2 7.0 1.0
OD1 A:ASN168 2.2 6.7 1.0
O8 A:BYN603 2.2 6.2 1.0
O A:HOH756 2.2 7.0 1.0
O A:HOH833 2.3 7.5 1.0
ND1 A:HIS191 2.3 6.6 1.0
CG A:ASN168 3.1 6.6 1.0
CD A:GLU233 3.2 6.5 1.0
CE1 A:HIS191 3.2 7.3 1.0
P1 A:BYN603 3.4 6.2 1.0
CG A:HIS191 3.4 6.2 1.0
ND2 A:ASN168 3.5 6.6 1.0
OE1 A:GLU233 3.5 6.8 1.0
O9 A:BYN603 3.6 6.9 1.0
K A:K602 3.7 7.0 1.0
CB A:HIS191 3.8 6.8 1.0
O10 A:BYN603 4.3 6.7 1.0
CG1 A:ILE227 4.3 8.8 1.0
CZ2 A:TRP166 4.4 9.0 1.0
O A:ILE227 4.4 7.5 1.0
NE2 A:HIS191 4.4 7.5 1.0
CG A:GLU233 4.5 7.1 1.0
O7 A:BYN603 4.5 6.8 1.0
CD2 A:HIS191 4.5 7.2 1.0
CB A:ASN168 4.5 6.9 1.0
O A:VAL231 4.5 8.1 1.0
O A:TRP169 4.6 6.5 1.0
NE1 A:TRP166 4.6 8.4 1.0
O A:PRO228 4.7 7.8 1.0
CE2 A:TRP166 4.9 8.3 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: Sun Oct 6 04:21:28 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy