Copper in PDB 5zpn: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (1)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (1)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (1):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 K (1), PDB code: 5zpn 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)*	39.66 / 1.60
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	192.715, 63.801, 158.805, 90.00, 116.99, 90.00
*R / R_free (%)*	18.4 / 20.8

Other elements in 5zpn:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 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 Phenylethylamine at pH 8 at 288 K (1) (pdb code 5zpn). 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 Phenylethylamine at pH 8 at 288 K (1), PDB code: 5zpn:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpn

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Copper Binding Sites List in 5zpn

Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 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 Phenylethylamine at pH 8 at 288 K (1) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu705 b:19.0 occ:1.00	NE2	A:HIS433	2.1	18.5	1.0
	NE2	A:HIS431	2.1	20.0	1.0
	ND1	A:HIS592	2.2	18.7	1.0
	O	A:HOH1173	2.3	27.4	0.7
	OH	A:TYQ382	2.7	19.9	0.7
	CD2	A:HIS433	3.0	19.6	1.0
	CD2	A:HIS431	3.0	19.2	1.0
	CE1	A:HIS431	3.1	19.6	1.0
	CG	A:HIS592	3.1	18.2	1.0
	CE1	A:HIS433	3.1	24.1	1.0
	CE1	A:HIS592	3.2	23.9	1.0
	CB	A:HIS592	3.3	17.8	1.0
	O	A:HOH1252	3.6	42.5	1.0
	CZ	A:TYQ382	3.6	22.0	0.7
	N5	A:TYQ382	4.2	29.6	0.7
	ND1	A:HIS431	4.2	19.8	1.0
	CG	A:HIS433	4.2	18.1	1.0
	CG	A:HIS431	4.2	20.9	1.0
	ND1	A:HIS433	4.2	20.4	1.0
	CE2	A:TYQ382	4.2	29.0	0.7
	CD2	A:HIS592	4.2	18.6	1.0
	NE2	A:HIS592	4.2	20.8	1.0
	CE1	A:TYQ382	4.4	23.9	0.7
	O	A:HOH876	4.5	18.4	1.0
	CE	A:MET602	4.7	45.5	1.0
	OZ	A:TYQ382	4.8	25.3	0.3
	CA	A:HIS592	4.9	17.6	1.0

Copper binding site 2 out of 2 in 5zpn

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Copper Binding Sites List in 5zpn

Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 8 at 288 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 Phenylethylamine at pH 8 at 288 K (1) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cu704 b:17.2 occ:1.00	CE1	B:HIS433	2.1	10.2	1.0
	NE2	B:HIS431	2.1	15.1	1.0
	ND1	B:HIS592	2.1	16.4	1.0
	O	B:HOH1228	2.3	17.4	0.5
	OH	B:TYQ382	2.7	16.8	0.7
	NE2	B:HIS433	3.0	19.4	1.0
	ND1	B:HIS433	3.0	23.8	1.0
	CE1	B:HIS431	3.1	16.7	1.0
	CG	B:HIS592	3.1	15.3	1.0
	CD2	B:HIS431	3.1	12.7	1.0
	CE1	B:HIS592	3.1	19.1	1.0
	CB	B:HIS592	3.3	13.4	1.0
	O	B:HOH1241	3.3	43.3	1.0
	CZ	B:TYQ382	3.5	21.3	0.7
	N5	B:TYQ382	4.0	25.4	0.7
	CE2	B:TYQ382	4.1	23.8	0.7
	ND1	B:HIS431	4.2	14.4	1.0
	CD2	B:HIS433	4.2	12.9	1.0
	NE2	B:HIS592	4.2	14.3	1.0
	CG	B:HIS431	4.2	12.4	1.0
	CD2	B:HIS592	4.2	13.9	1.0
	CG	B:HIS433	4.2	15.4	1.0
	CE1	B:TYQ382	4.4	18.4	0.7
	O	B:HOH842	4.4	18.1	1.0
	OZ	B:TYQ382	4.6	20.1	0.3
	CA	B:HIS592	4.9	13.5	1.0
	SD	B:MET602	4.9	25.7	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 05:51:20 2025

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