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Manganese in PDB 6r2p: Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid

Enzymatic activity of Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid

All present enzymatic activity of Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid:
4.1.1.102;

Protein crystallography data

The structure of Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid, PDB code: 6r2p was solved by S.S.Bailey, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.14 / 1.26
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.895, 63.835, 87.651, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.7

Other elements in 6r2p:

The structure of Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid also contains other interesting chemical elements:

Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid (pdb code 6r2p). 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 Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid, PDB code: 6r2p:

Manganese binding site 1 out of 1 in 6r2p

Go back to Manganese Binding Sites List in 6r2p
Manganese binding site 1 out of 1 in the Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Aspergillus Niger Ferulic Acid Decarboxylase (Fdc) in Complex with Fmn and Cinnamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn602

b:6.3
occ:1.00
 OE2 A:GLU233 2.1 6.4 1.0
OD1 A:ASN168 2.2 6.0 1.0
O A:HOH727 2.2 6.0 1.0
O2P A:FMN601 2.2 5.3 1.0
O A:HOH825 2.3 6.7 1.0
ND1 A:HIS191 2.3 6.4 1.0
CD A:GLU233 3.1 5.4 1.0
CG A:ASN168 3.1 6.8 1.0
CE1 A:HIS191 3.2 6.6 1.0
P A:FMN601 3.4 5.6 1.0
CG A:HIS191 3.4 5.8 1.0
ND2 A:ASN168 3.5 6.7 1.0
OE1 A:GLU233 3.5 6.4 1.0
O3P A:FMN601 3.6 5.9 1.0
K A:K603 3.7 6.5 1.0
CB A:HIS191 3.8 7.0 1.0
O1P A:FMN601 4.3 6.1 1.0
CG1 A:ILE227 4.4 8.0 1.0
CZ2 A:TRP166 4.4 7.5 1.0
O A:ILE227 4.4 7.7 1.0
NE2 A:HIS191 4.4 6.4 1.0
O A:VAL231 4.5 8.4 1.0
O5' A:FMN601 4.5 6.2 1.0
CB A:ASN168 4.5 6.8 1.0
CD2 A:HIS191 4.5 7.0 1.0
CG A:GLU233 4.5 6.4 1.0
O A:TRP169 4.6 6.9 1.0
NE1 A:TRP166 4.6 8.0 1.0
O A:PRO228 4.7 7.5 1.0
CE2 A:TRP166 4.9 8.0 1.0
CA A:ASN168 5.0 5.7 1.0

Reference:

S.S.Bailey, K.A.P.Payne, A.Saaret, S.A.Marshall, I.Gostimskaya, I.Kosov, K.Fisher, S.Hay, D.Leys. Atomic Description of An Enzyme Reaction Dependent on Reversible 1,3-Dipolar Cycloaddition To Be Published.
Page generated: Sun Oct 6 06:57:44 2024

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