Manganese in PDB 4za9: Structure of A. Niger FDC1 in Complex with A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor

Enzymatic activity of Structure of A. Niger FDC1 in Complex with A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor

All present enzymatic activity of Structure of A. Niger FDC1 in Complex with A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor:
4.1.1.61;

Protein crystallography data

The structure of Structure of A. Niger FDC1 in Complex with A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor, PDB code: 4za9 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)*	63.85 / 1.01
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	96.050, 63.850, 87.680, 90.00, 90.00, 90.00
*R / R_free (%)*	13 / 14.5

Other elements in 4za9:

The structure of Structure of A. Niger FDC1 in Complex with A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor 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 A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor (pdb code 4za9). 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 A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor, PDB code: 4za9:

Manganese binding site 1 out of 1 in 4za9

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Manganese Binding Sites List in 4za9

Manganese binding site 1 out of 1 in the Structure of A. Niger FDC1 in Complex with A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor

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 A Phenylpyruvate Derived Adduct to the Prenylated Flavin Cofactor within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn602 b:7.2 occ:1.00	OE2	A:GLU233	2.1	6.4	1.0
	OD1	A:ASN168	2.1	6.7	1.0
	O	A:HOH733	2.2	6.9	1.0
	O	A:HOH823	2.2	7.6	1.0
	O2	A:4MJ601	2.2	5.7	1.0
	ND1	A:HIS191	2.3	6.8	1.0
	CG	A:ASN168	3.1	6.6	1.0
	CD	A:GLU233	3.2	6.5	1.0
	CE1	A:HIS191	3.2	7.0	1.0
	CG	A:HIS191	3.4	6.4	1.0
	P1	A:4MJ601	3.4	5.6	1.0
	ND2	A:ASN168	3.5	6.8	1.0
	OE1	A:GLU233	3.5	6.9	1.0
	O3	A:4MJ601	3.6	6.2	1.0
	K	A:K603	3.7	6.9	1.0
	CB	A:HIS191	3.8	6.6	1.0
	O1	A:4MJ601	4.3	6.3	1.0
	CZ2	A:TRP166	4.3	8.4	1.0
	O	A:ILE227	4.3	7.1	1.0
	CG1	A:ILE227	4.3	8.4	1.0
	NE2	A:HIS191	4.4	7.3	1.0
	O	A:VAL231	4.5	8.3	1.0
	O4	A:4MJ601	4.5	5.9	1.0
	CD2	A:HIS191	4.5	7.3	1.0
	CB	A:ASN168	4.5	6.8	1.0
	CG	A:GLU233	4.5	6.9	1.0
	O	A:TRP169	4.6	6.5	1.0
	NE1	A:TRP166	4.6	8.3	1.0
	O	A:PRO228	4.7	8.0	1.0
	CE2	A:TRP166	4.9	7.7	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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