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Manganese in PDB 4za7: Structure of A. Niger FDC1 in Complex with Alpha-Methyl Cinnamic Acid

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

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

Protein crystallography data

The structure of Structure of A. Niger FDC1 in Complex with Alpha-Methyl Cinnamic Acid, PDB code: 4za7 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) 30.05 / 1.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.940, 64.170, 87.730, 90.00, 90.00, 90.00
R / Rfree (%) 13.2 / 14

Other elements in 4za7:

The structure of Structure of A. Niger FDC1 in Complex with Alpha-Methyl Cinnamic Acid 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 Alpha-Methyl Cinnamic Acid (pdb code 4za7). 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-Methyl Cinnamic Acid, PDB code: 4za7:

Manganese binding site 1 out of 1 in 4za7

Go back to Manganese Binding Sites List in 4za7
Manganese binding site 1 out of 1 in the Structure of A. Niger FDC1 in Complex with Alpha-Methyl 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-Methyl Cinnamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn603

b:7.5
occ:1.00
 OD1 A:ASN168 2.1 7.2 1.0
OE2 A:GLU233 2.1 7.3 1.0
O8 A:FZZ602 2.2 7.7 0.5
O2P A:4LU601 2.2 6.6 0.5
O A:HOH728 2.2 7.9 1.0
O A:HOH818 2.2 8.4 1.0
ND1 A:HIS191 2.3 7.1 1.0
CG A:ASN168 3.1 7.2 1.0
CD A:GLU233 3.2 7.4 1.0
CE1 A:HIS191 3.2 7.3 1.0
CG A:HIS191 3.4 7.0 1.0
P A:4LU601 3.4 6.6 0.5
P1 A:FZZ602 3.4 6.9 0.5
ND2 A:ASN168 3.5 7.6 1.0
OE1 A:GLU233 3.5 7.8 1.0
O7 A:FZZ602 3.6 9.3 0.5
O3P A:4LU601 3.6 7.6 0.5
K A:K604 3.7 8.0 1.0
CB A:HIS191 3.8 7.6 1.0
O9 A:FZZ602 4.3 7.4 0.5
O1P A:4LU601 4.3 8.0 0.5
O A:ILE227 4.3 8.2 1.0
CZ2 A:TRP166 4.4 8.9 1.0
NE2 A:HIS191 4.4 7.8 1.0
CG1 A:ILE227 4.4 10.2 1.0
O A:VAL231 4.5 8.9 1.0
CB A:ASN168 4.5 7.3 1.0
O5' A:4LU601 4.5 6.5 0.5
O6 A:FZZ602 4.5 8.1 0.5
CD2 A:HIS191 4.5 7.9 1.0
CG A:GLU233 4.5 7.9 1.0
O A:TRP169 4.6 7.0 1.0
NE1 A:TRP166 4.6 9.5 1.0
O A:PRO228 4.7 8.8 1.0
CE2 A:TRP166 4.9 8.5 1.0
CA A:ASN168 5.0 6.8 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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