Sodium in PDB 5zpg: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1), PDB code: 5zpg was solved by T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, K.Tanizawa, T.Kumasaka, M.Yamamoto, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	38.88 / 1.65
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	193.283, 64.012, 158.812, 90.00, 117.04, 90.00
*R / R_free (%)*	16.3 / 18.4

Other elements in 5zpg:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1) also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1) (pdb code 5zpg). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1), PDB code: 5zpg:

Sodium binding site 1 out of 1 in 5zpg

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Sodium Binding Sites List in 5zpg

Sodium binding site 1 out of 1 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1)

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at PH6 at 293K (1) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Na702 b:11.3 occ:1.00	OD1	B:ASP581	2.4	19.4	1.0
	OD1	B:ASP440	2.4	17.6	1.0
	O	B:MET441	2.5	16.5	1.0
	O	B:ILE582	2.6	14.9	1.0
	O	B:HOH1012	2.8	18.5	1.0
	N	B:ILE582	3.3	13.5	1.0
	N	B:MET441	3.4	13.0	1.0
	C	B:MET441	3.5	15.7	1.0
	C	B:ILE582	3.5	13.3	1.0
	CG	B:ASP581	3.6	22.7	1.0
	CG	B:ASP440	3.7	16.3	1.0
	NH2	B:ARG49	3.8	31.0	1.0
	C	B:ASP581	3.8	15.3	1.0
	C	B:ASP440	3.9	14.8	1.0
	CD1	B:PHE446	3.9	23.3	1.0
	CA	B:ILE582	4.0	13.4	1.0
	CA	B:MET441	4.0	13.3	1.0
	CA	B:ASP581	4.1	15.3	1.0
	CE1	B:PHE446	4.3	27.2	1.0
	CA	B:ASP440	4.4	11.9	1.0
	OD2	B:ASP440	4.4	16.6	1.0
	CB	B:ASP581	4.5	17.7	1.0
	O	B:ASP440	4.5	14.8	1.0
	OD2	B:ASP581	4.5	26.0	1.0
	CB	B:MET441	4.6	14.1	1.0
	CB	B:ASP440	4.6	15.0	1.0
	O	B:ASP581	4.7	17.2	1.0
	N	B:VAL583	4.7	12.2	1.0
	N	B:ALA442	4.7	12.5	1.0
	CG2	B:VAL583	4.8	13.2	1.0
	CB	B:TYR546	4.8	15.7	1.0
	CG1	B:ILE582	5.0	19.8	1.0

Reference:

T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, T.Kumasaka, M.Yamamoto, K.Tanizawa, T.Okajima. In Crystallothermodynamic Analysis of Conformational Change of the Topaquinone Cofactor in Bacterial Copper Amine Oxidase Proc. Natl. Acad. Sci. V. 116 135 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30563857
DOI: 10.1073/PNAS.1811837116

Page generated: Tue Oct 8 01:37:53 2024

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