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Manganese in PDB 4za4: Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.

Enzymatic activity of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.

All present enzymatic activity of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.:
4.1.1.61;

Protein crystallography data

The structure of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form., PDB code: 4za4 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) 33.82 / 1.22
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.990, 63.930, 87.630, 90.00, 90.00, 90.00
R / Rfree (%) 14.6 / 16.1

Other elements in 4za4:

The structure of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form. 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 with the Prenylated-Flavin Cofactor in the Iminium Form. (pdb code 4za4). 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 with the Prenylated-Flavin Cofactor in the Iminium Form., PDB code: 4za4:

Manganese binding site 1 out of 1 in 4za4

Go back to Manganese Binding Sites List in 4za4
Manganese binding site 1 out of 1 in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.


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 with the Prenylated-Flavin Cofactor in the Iminium Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn602

b:7.3
occ:1.00
 OE2 A:GLU233 2.1 7.5 1.0
OD1 A:ASN168 2.1 6.9 1.0
O2P A:4LU601 2.2 6.8 1.0
O A:HOH727 2.2 7.6 1.0
O A:HOH794 2.3 8.0 1.0
ND1 A:HIS191 2.3 8.2 1.0
CG A:ASN168 3.1 7.1 1.0
CE1 A:HIS191 3.2 6.9 1.0
CD A:GLU233 3.2 7.2 1.0
CG A:HIS191 3.4 7.0 1.0
P A:4LU601 3.4 6.6 1.0
ND2 A:ASN168 3.5 7.5 1.0
OE1 A:GLU233 3.5 7.6 1.0
O3P A:4LU601 3.6 7.3 1.0
K A:K603 3.7 7.7 1.0
CB A:HIS191 3.7 7.4 1.0
O1P A:4LU601 4.3 7.7 1.0
O A:ILE227 4.3 7.5 1.0
CZ2 A:TRP166 4.3 8.9 1.0
NE2 A:HIS191 4.4 7.8 1.0
CG1 A:ILE227 4.4 9.4 1.0
CG A:GLU233 4.5 7.8 1.0
CD2 A:HIS191 4.5 7.8 1.0
O A:VAL231 4.5 8.6 1.0
CB A:ASN168 4.5 7.2 1.0
O5' A:4LU601 4.5 7.0 1.0
O A:TRP169 4.6 6.7 1.0
NE1 A:TRP166 4.6 9.1 1.0
O A:PRO228 4.7 8.2 1.0
CE2 A:TRP166 4.9 8.2 1.0
CA A:ASN168 5.0 6.6 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: Tue Dec 15 04:34:25 2020

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