Manganese in PDB 6ev4: Structure of Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form

Enzymatic activity of Structure of Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form

All present enzymatic activity of Structure of Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form:
4.1.1.102;

Protein crystallography data

The structure of Structure of Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form, PDB code: 6ev4 was solved by S.S.Bailey, L.David, K.A.P.Payne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	47.98 / 1.14
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	95.970, 64.030, 87.630, 90.00, 90.00, 90.00
*R / R_free (%)*	14.9 / 16.7

Other elements in 6ev4:

The structure of Structure of Wild Type A. Niger FDC1 Purified in the Dark with Prfmn 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 Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form (pdb code 6ev4). 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 Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form, PDB code: 6ev4:

Manganese binding site 1 out of 1 in 6ev4

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Manganese Binding Sites List in 6ev4

Manganese binding site 1 out of 1 in the Structure of Wild Type A. Niger FDC1 Purified in the Dark with Prfmn 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 Wild Type A. Niger FDC1 Purified in the Dark with Prfmn in the Iminium Form within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn602 b:7.4 occ:1.00	OE2	A:GLU233	2.1	6.7	1.0
	OD1	A:ASN168	2.1	6.5	1.0
	O2P	A:4LU601	2.2	6.3	1.0
	O	A:HOH777	2.2	6.7	1.0
	O	A:HOH925	2.2	7.1	1.0
	ND1	A:HIS191	2.3	6.6	1.0
	CG	A:ASN168	3.1	6.4	1.0
	CD	A:GLU233	3.2	6.6	1.0
	CE1	A:HIS191	3.2	6.9	1.0
	P	A:4LU601	3.4	6.0	1.0
	CG	A:HIS191	3.4	6.2	1.0
	ND2	A:ASN168	3.5	6.7	1.0
	OE1	A:GLU233	3.5	7.2	1.0
	O3P	A:4LU601	3.6	6.5	1.0
	K	A:K603	3.7	7.8	1.0
	CB	A:HIS191	3.8	6.5	1.0
	O1P	A:4LU601	4.2	6.6	1.0
	CZ2	A:TRP166	4.3	7.9	1.0
	O	A:ILE227	4.3	6.9	1.0
	NE2	A:HIS191	4.4	6.7	1.0
	CG1	A:ILE227	4.4	8.7	1.0
	CD2	A:HIS191	4.5	6.6	1.0
	CB	A:ASN168	4.5	6.8	1.0
	CG	A:GLU233	4.5	6.3	1.0
	O5'	A:4LU601	4.5	6.2	1.0
	O	A:VAL231	4.5	7.8	1.0
	O	A:TRP169	4.6	6.4	1.0
	NE1	A:TRP166	4.6	7.8	1.0
	O	A:PRO228	4.7	7.1	1.0
	CE2	A:TRP166	4.9	7.8	1.0
	CA	A:ASN168	5.0	6.3	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 04:20:30 2024

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