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Manganese in PDB 4zaa: Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol

Enzymatic activity of Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol

All present enzymatic activity of Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol:
4.1.1.61;

Protein crystallography data

The structure of Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol, PDB code: 4zaa was solved by K.A.P.Payne, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 94.19 / 1.24
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.592, 64.467, 87.885, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 16.3

Other elements in 4zaa:

The structure of Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol also contains other interesting chemical elements:

Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol (pdb code 4zaa). 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 A. Niger FDC1 in Complex with 4-Vinyl Guaiacol, PDB code: 4zaa:

Manganese binding site 1 out of 1 in 4zaa

Go back to Manganese Binding Sites List in 4zaa
Manganese binding site 1 out of 1 in the Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of A. Niger FDC1 in Complex with 4-Vinyl Guaiacol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn603

b:8.6
occ:1.00
OE2 A:GLU233 2.1 8.7 1.0
OD1 A:ASN168 2.2 8.4 1.0
O2P A:4LU601 2.2 7.8 0.5
O8 A:FZZ602 2.2 8.7 0.5
O A:HOH724 2.2 8.4 1.0
O A:HOH816 2.2 9.5 1.0
ND1 A:HIS191 2.3 8.9 1.0
CG A:ASN168 3.1 7.9 1.0
CD A:GLU233 3.2 8.7 1.0
CE1 A:HIS191 3.2 8.1 1.0
P A:4LU601 3.4 8.2 0.5
CG A:HIS191 3.4 8.2 1.0
P1 A:FZZ602 3.4 8.6 0.5
ND2 A:ASN168 3.5 8.4 1.0
OE1 A:GLU233 3.5 8.9 1.0
O7 A:FZZ602 3.6 10.2 0.5
O3P A:4LU601 3.6 9.1 0.5
K A:K604 3.7 9.1 1.0
CB A:HIS191 3.8 9.0 1.0
O9 A:FZZ602 4.3 9.3 0.5
O1P A:4LU601 4.3 10.1 0.5
O A:ILE227 4.4 8.8 1.0
CG1 A:ILE227 4.4 10.2 1.0
NE2 A:HIS191 4.4 9.5 1.0
CZ2 A:TRP166 4.4 10.5 1.0
O A:VAL231 4.5 9.7 1.0
CG A:GLU233 4.5 8.6 1.0
CD2 A:HIS191 4.5 9.4 1.0
O5' A:4LU601 4.5 9.0 0.5
O6 A:FZZ602 4.5 10.2 0.5
CB A:ASN168 4.5 8.4 1.0
O A:TRP169 4.6 8.2 1.0
NE1 A:TRP166 4.6 10.5 1.0
O A:PRO228 4.7 9.3 1.0
CE2 A:TRP166 4.9 9.6 1.0

Reference:

K.A.Payne, M.D.White, K.Fisher, B.Khara, S.S.Bailey, D.Parker, N.J.Rattray, D.K.Trivedi, R.Goodacre, R.Beveridge, P.Barran, S.E.Rigby, N.S.Scrutton, S.Hay, D.Leys. New Cofactor Supports Alpha , Beta-Unsaturated Acid Decarboxylation Via 1,3-Dipolar Cycloaddition. Nature V. 522 502 2015.
ISSN: ESSN 1476-4687
PubMed: 26083754
DOI: 10.1038/NATURE14560
Page generated: Sat Oct 5 23:12:11 2024

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