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Manganese in PDB 4za8: Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid

Enzymatic activity of Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid

All present enzymatic activity of Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid:
4.1.1.61;

Protein crystallography data

The structure of Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid, PDB code: 4za8 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) 64.81 / 1.06
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.010, 63.930, 87.840, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 16.6

Other elements in 4za8:

The structure of Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid also contains other interesting chemical elements:

Fluorine (F) 5 atoms
Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid (pdb code 4za8). 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 Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid, PDB code: 4za8:

Manganese binding site 1 out of 1 in 4za8

Go back to Manganese Binding Sites List in 4za8
Manganese binding site 1 out of 1 in the Crystal Structure of A Niger FDC1 in Complex with Penta-Fluorocinnamic Acid


Mono view


Stereo pair view

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

b:7.8
occ:1.00
 OD1 A:ASN168 2.1 7.3 1.0
OE2 A:GLU233 2.1 7.7 1.0
O2P A:4LU601 2.2 7.2 0.5
O8 A:FZZ602 2.2 8.3 0.5
O A:HOH722 2.2 7.9 1.0
O A:HOH829 2.2 8.3 1.0
ND1 A:HIS191 2.3 8.0 1.0
CG A:ASN168 3.1 7.3 1.0
CD A:GLU233 3.2 7.3 1.0
CE1 A:HIS191 3.2 7.7 1.0
CG A:HIS191 3.4 7.5 1.0
P A:4LU601 3.4 7.4 0.5
P1 A:FZZ602 3.4 7.7 0.5
O7 A:FZZ602 3.5 10.5 0.5
ND2 A:ASN168 3.5 7.9 1.0
OE1 A:GLU233 3.5 8.0 1.0
O3P A:4LU601 3.6 7.9 0.5
K A:K604 3.6 8.4 1.0
CB A:HIS191 3.8 8.0 1.0
O9 A:FZZ602 4.3 8.2 0.5
O A:ILE227 4.3 8.0 1.0
O1P A:4LU601 4.3 9.1 0.5
CZ2 A:TRP166 4.4 9.4 1.0
CG1 A:ILE227 4.4 9.7 1.0
NE2 A:HIS191 4.4 8.2 1.0
O6 A:FZZ602 4.5 9.3 0.5
O5' A:4LU601 4.5 7.8 0.5
O A:VAL231 4.5 9.0 1.0
CB A:ASN168 4.5 7.6 1.0
CG A:GLU233 4.5 7.7 1.0
CD2 A:HIS191 4.5 8.0 1.0
O A:TRP169 4.6 7.1 1.0
NE1 A:TRP166 4.6 9.5 1.0
O A:PRO228 4.7 8.7 1.0
CE2 A:TRP166 4.9 8.6 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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