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Manganese in PDB 6ev6: Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms

Enzymatic activity of Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms

All present enzymatic activity of Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms:
4.1.1.102;

Protein crystallography data

The structure of Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms, PDB code: 6ev6 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) 53.07 / 1.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.050, 63.680, 87.790, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 16.9

Other elements in 6ev6:

The structure of Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms also contains other interesting chemical elements:

Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms (pdb code 6ev6). 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 E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms, PDB code: 6ev6:

Manganese binding site 1 out of 1 in 6ev6

Go back to Manganese Binding Sites List in 6ev6
Manganese binding site 1 out of 1 in the Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated and Ketimine Forms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:9.8
occ:1.00
 OD1 A:ASN168 2.1 9.2 1.0
OE2 A:GLU233 2.1 9.8 1.0
O8 A:BYN605 2.2 5.7 0.5
O7 A:FZZ604 2.2 15.7 0.5
O A:HOH784 2.2 9.7 1.0
O A:HOH917 2.2 10.2 1.0
ND1 A:HIS191 2.3 10.2 1.0
CG A:ASN168 3.1 9.2 1.0
CE1 A:HIS191 3.2 10.1 1.0
CD A:GLU233 3.2 9.3 1.0
P1 A:FZZ604 3.4 17.1 0.5
CG A:HIS191 3.4 9.5 1.0
P1 A:BYN605 3.4 5.6 0.5
ND2 A:ASN168 3.5 9.7 1.0
OE1 A:GLU233 3.6 9.9 1.0
O10 A:BYN605 3.6 7.0 0.5
O9 A:FZZ604 3.6 17.2 0.5
K A:K602 3.7 10.6 1.0
CB A:HIS191 3.8 9.8 1.0
O A:HOH708 3.8 1.0 1.0
O6 A:FZZ604 4.1 16.2 0.5
O9 A:BYN605 4.3 6.7 0.5
CZ2 A:TRP166 4.3 11.1 1.0
O A:ILE227 4.3 10.1 1.0
NE2 A:HIS191 4.4 10.5 1.0
CG1 A:ILE227 4.4 11.6 1.0
O8 A:FZZ604 4.4 15.7 0.5
CD2 A:HIS191 4.5 10.4 1.0
CB A:ASN168 4.5 9.3 1.0
CG A:GLU233 4.5 9.6 1.0
O A:VAL231 4.5 11.0 1.0
O7 A:BYN605 4.5 5.8 0.5
NE1 A:TRP166 4.6 11.1 1.0
O A:TRP169 4.6 9.3 1.0
O A:PRO228 4.7 10.8 1.0
CE2 A:TRP166 4.8 10.7 1.0
CA A:ASN168 5.0 9.2 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 04:20:42 2024

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