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Manganese in PDB 4zab: Structure of A. Niger FDC1 in Complex with Alpha-Fluoro Cinnamic Acid

Enzymatic activity of Structure of A. Niger FDC1 in Complex with Alpha-Fluoro Cinnamic Acid

All present enzymatic activity of Structure of A. Niger FDC1 in Complex with Alpha-Fluoro Cinnamic Acid:
4.1.1.61;

Protein crystallography data

The structure of Structure of A. Niger FDC1 in Complex with Alpha-Fluoro Cinnamic Acid, PDB code: 4zab 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) 32.28 / 1.16
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.910, 64.200, 87.790, 90.00, 90.00, 90.00
R / Rfree (%) 14.6 / 15.4

Other elements in 4zab:

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

Fluorine (F) 1 atom
Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of A. Niger FDC1 in Complex with Alpha-Fluoro Cinnamic Acid (pdb code 4zab). 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 Alpha-Fluoro Cinnamic Acid, PDB code: 4zab:

Manganese binding site 1 out of 1 in 4zab

Go back to Manganese Binding Sites List in 4zab
Manganese binding site 1 out of 1 in the Structure of A. Niger FDC1 in Complex with Alpha-Fluoro Cinnamic Acid


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 Alpha-Fluoro Cinnamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn603

b:7.2
occ:1.00
 OD1 A:ASN168 2.1 6.9 1.0
OE2 A:GLU233 2.1 7.0 1.0
O2P A:4LU601 2.2 6.3 0.5
O8 A:FZZ602 2.2 7.4 0.5
O A:HOH726 2.2 7.2 1.0
O A:HOH835 2.2 7.8 1.0
ND1 A:HIS191 2.3 7.6 1.0
CG A:ASN168 3.1 7.1 1.0
CD A:GLU233 3.2 6.9 1.0
CE1 A:HIS191 3.2 6.7 1.0
CG A:HIS191 3.4 6.7 1.0
P A:4LU601 3.4 6.5 0.5
P1 A:FZZ602 3.4 6.8 0.5
ND2 A:ASN168 3.5 7.3 1.0
OE1 A:GLU233 3.5 7.3 1.0
O7 A:FZZ602 3.5 8.9 0.5
O3P A:4LU601 3.6 7.0 0.5
K A:K604 3.7 7.5 1.0
CB A:HIS191 3.7 7.5 1.0
O9 A:FZZ602 4.3 7.1 0.5
O1P A:4LU601 4.3 7.7 0.5
CZ2 A:TRP166 4.3 8.3 1.0
O A:ILE227 4.3 7.3 1.0
CG1 A:ILE227 4.4 9.2 1.0
NE2 A:HIS191 4.4 7.5 1.0
O5' A:4LU601 4.5 6.6 0.5
O6 A:FZZ602 4.5 8.3 0.5
O A:VAL231 4.5 8.4 1.0
CB A:ASN168 4.5 7.0 1.0
CG A:GLU233 4.5 7.1 1.0
CD2 A:HIS191 4.5 7.3 1.0
O A:TRP169 4.6 6.5 1.0
NE1 A:TRP166 4.6 9.1 1.0
O A:PRO228 4.7 8.1 1.0
CE2 A:TRP166 4.9 7.7 1.0
CA A:ASN168 5.0 6.4 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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