Copper in PDB 5zp5: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1), PDB code: 5zp5 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)*	35.33 / 1.77
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	193.724, 64.816, 158.820, 90.00, 117.15, 90.00
*R / R_free (%)*	16.7 / 19.8

Other elements in 5zp5:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1) also contains other interesting chemical elements:

Sodium

(Na)

3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1) (pdb code 5zp5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1), PDB code: 5zp5:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp5

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Copper Binding Sites List in 5zp5

Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1)

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu701 b:16.3 occ:1.00	O	A:HOH890	1.9	23.2	0.9
	NE2	A:HIS431	2.0	13.4	1.0
	NE2	A:HIS433	2.1	14.4	1.0
	ND1	A:HIS592	2.1	16.1	1.0
	OH	A:TYQ382	2.5	9.1	0.5
	O	A:HOH801	2.8	14.7	0.0
	CD2	A:HIS431	3.0	11.7	1.0
	CE1	A:HIS431	3.0	12.3	1.0
	CD2	A:HIS433	3.1	14.4	1.0
	CE1	A:HIS592	3.1	18.9	1.0
	CG	A:HIS592	3.1	15.4	1.0
	CE1	A:HIS433	3.1	14.7	1.0
	CZ	A:TYQ382	3.4	22.8	0.5
	CB	A:HIS592	3.4	14.2	1.0
	CE1	A:TYQ382	4.0	28.9	0.5
	ND1	A:HIS431	4.1	10.4	1.0
	CG	A:HIS431	4.1	10.7	1.0
	NE2	A:HIS592	4.2	16.8	1.0
	ND1	A:HIS433	4.2	13.2	1.0
	CE2	A:TYQ382	4.2	29.8	0.5
	CG	A:HIS433	4.2	12.6	1.0
	CD2	A:HIS592	4.2	16.1	1.0
	O	A:HOH867	4.3	17.4	1.0
	N5	A:TYQ382	4.3	37.4	0.5
	OZ	A:TYQ382	4.9	23.7	0.5
	SD	A:MET602	4.9	28.7	1.0
	CA	A:HIS592	4.9	12.4	1.0

Copper binding site 2 out of 2 in 5zp5

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Copper Binding Sites List in 5zp5

Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1)

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 6 at 277 K (1) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cu701 b:16.4 occ:1.00	O	B:HOH822	2.0	22.4	0.7
	NE2	B:HIS431	2.0	13.4	1.0
	ND1	B:HIS592	2.0	14.1	1.0
	NE2	B:HIS433	2.1	12.6	1.0
	O	B:HOH1086	2.3	22.8	0.7
	OH	B:TYQ382	2.4	29.2	0.5
	CD2	B:HIS431	2.9	10.7	1.0
	CE1	B:HIS592	2.9	17.8	1.0
	CE1	B:HIS431	3.0	17.3	1.0
	CG	B:HIS592	3.1	21.0	1.0
	CE1	B:HIS433	3.1	17.1	1.0
	CD2	B:HIS433	3.1	10.8	1.0
	CZ	B:TYQ382	3.3	28.6	0.5
	CB	B:HIS592	3.4	11.2	1.0
	O	B:HOH1257	3.6	38.1	1.0
	CE2	B:TYQ382	3.9	35.5	0.5
	N5	B:TYQ382	3.9	42.2	0.5
	CE1	B:TYQ382	4.1	28.9	0.5
	OZ	B:TYQ382	4.1	32.1	0.5
	ND1	B:HIS431	4.1	11.5	1.0
	CG	B:HIS431	4.1	8.3	1.0
	NE2	B:HIS592	4.1	13.7	1.0
	CD2	B:HIS592	4.2	14.8	1.0
	ND1	B:HIS433	4.2	12.0	1.0
	CG	B:HIS433	4.2	11.4	1.0
	O	B:HOH850	4.3	15.8	1.0
	SD	B:MET602	4.9	27.3	1.0
	CA	B:HIS592	5.0	11.8	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: Mon Jul 14 05:49:02 2025

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