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Manganese in PDB 6ev5: Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form

Enzymatic activity of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form

All present enzymatic activity of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form:
4.1.1.102;

Protein crystallography data

The structure of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6ev5 was solved by S.S.Bailey, D.Leys, K.A.P.Payne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.30 / 1.28
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 96.020, 63.510, 87.620, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19

Other elements in 6ev5:

The structure of Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form also contains other interesting chemical elements:

Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form (pdb code 6ev5). 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 E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form, PDB code: 6ev5:

Manganese binding site 1 out of 1 in 6ev5

Go back to Manganese Binding Sites List in 6ev5
Manganese binding site 1 out of 1 in the Crystal Structure of E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form


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 E282Q A. Niger FDC1 with Prfmn in the Hydroxylated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:9.9
occ:1.00
 OE2 A:GLU233 2.1 10.0 1.0
OD1 A:ASN168 2.2 8.6 1.0
O A:HOH752 2.2 8.6 1.0
O8 A:BYN604 2.2 8.6 1.0
O A:HOH867 2.2 8.4 1.0
ND1 A:HIS191 2.3 9.7 1.0
CG A:ASN168 3.1 8.3 1.0
CD A:GLU233 3.2 9.7 1.0
CE1 A:HIS191 3.2 8.8 1.0
P1 A:BYN604 3.4 8.7 1.0
CG A:HIS191 3.4 9.5 1.0
ND2 A:ASN168 3.5 10.2 1.0
OE1 A:GLU233 3.5 11.0 1.0
O9 A:BYN604 3.6 10.4 1.0
K A:K602 3.7 11.0 1.0
CB A:HIS191 3.8 9.8 1.0
O10 A:BYN604 4.2 10.7 1.0
O A:ILE227 4.3 10.1 1.0
CZ2 A:TRP166 4.3 11.3 1.0
CG1 A:ILE227 4.3 12.9 1.0
NE2 A:HIS191 4.4 9.6 1.0
CB A:ASN168 4.4 9.0 1.0
CD2 A:HIS191 4.5 9.2 1.0
O7 A:BYN604 4.5 9.4 1.0
CG A:GLU233 4.5 10.9 1.0
O A:VAL231 4.5 11.2 1.0
O A:TRP169 4.6 9.4 1.0
NE1 A:TRP166 4.6 11.1 1.0
O A:PRO228 4.7 11.8 1.0
CE2 A:TRP166 4.9 10.5 1.0

Reference:

S.S.Bailey, K.A.P.Payne, K.Fisher, S.A.Marshall, M.J.Cliff, R.Spiess, D.A.Parker, S.E.J.Rigby, D.Leys. The Role of Conserved Residues in Fdc Decarboxylase in Prenylated Flavin Mononucleotide Oxidative Maturation, Cofactor Isomerization, and Catalysis. J. Biol. Chem. V. 293 2272 2018.
ISSN: ESSN 1083-351X
PubMed: 29259125
DOI: 10.1074/JBC.RA117.000881
Page generated: Sun Oct 6 04:20:40 2024

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