Copper in PDB 5zp2: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2), PDB code: 5zp2 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)*	34.64 / 1.75
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	193.765, 64.920, 158.953, 90.00, 117.16, 90.00
*R / R_free (%)*	15.1 / 17.5

Other elements in 5zp2:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2) 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 9 at 288 K (2) (pdb code 5zp2). 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 9 at 288 K (2), PDB code: 5zp2:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zp2

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Copper Binding Sites List in 5zp2

Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2)

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 9 at 288 K (2) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu701 b:17.9 occ:1.00	NE2	A:HIS431	2.0	13.0	1.0
	O	A:HOH803	2.0	21.1	0.8
	NE2	A:HIS433	2.1	12.1	1.0
	ND1	A:HIS592	2.1	18.3	1.0
	OH	A:TYQ382	2.3	29.6	0.8
	O	A:HOH1135	2.5	12.8	0.3
	CE1	A:HIS431	3.0	15.7	1.0
	CD2	A:HIS431	3.0	12.1	1.0
	CE1	A:HIS433	3.0	15.2	1.0
	CE1	A:HIS592	3.0	20.0	1.0
	CD2	A:HIS433	3.1	13.6	1.0
	CG	A:HIS592	3.1	17.8	1.0
	CZ	A:TYQ382	3.3	30.3	0.8
	CB	A:HIS592	3.4	13.3	1.0
	N5	A:TYQ382	3.8	47.7	0.8
	CE2	A:TYQ382	3.9	40.0	0.8
	ND1	A:HIS431	4.1	14.1	1.0
	CG	A:HIS431	4.1	12.4	1.0
	ND1	A:HIS433	4.1	12.1	1.0
	NE2	A:HIS592	4.1	17.3	1.0
	CG	A:HIS433	4.2	12.2	1.0
	CD2	A:HIS592	4.2	19.0	1.0
	CE1	A:TYQ382	4.2	30.4	0.8
	OZ	A:TYQ382	4.3	31.9	0.2
	O	A:HOH943	4.3	19.4	1.0
	CE	A:MET602	4.5	25.6	0.1
	SD	A:MET602	4.9	26.7	0.9
	CA	A:HIS592	5.0	14.2	1.0

Copper binding site 2 out of 2 in 5zp2

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Copper Binding Sites List in 5zp2

Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Ethylamine at pH 9 at 288 K (2)

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 9 at 288 K (2) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cu701 b:18.3 occ:1.00	NE2	B:HIS431	2.0	13.5	1.0
	O	B:HOH803	2.0	17.1	0.5
	ND1	B:HIS592	2.0	19.4	1.0
	NE2	B:HIS433	2.1	13.6	1.0
	OH	B:TYQ382	2.4	20.6	0.8
	CD2	B:HIS431	2.9	13.3	1.0
	CE1	B:HIS592	3.0	20.7	1.0
	CE1	B:HIS433	3.0	14.3	1.0
	CE1	B:HIS431	3.0	19.4	1.0
	CG	B:HIS592	3.1	18.4	1.0
	CD2	B:HIS433	3.1	12.7	1.0
	CZ	B:TYQ382	3.2	20.0	0.8
	CB	B:HIS592	3.4	15.4	1.0
	N5	B:TYQ382	3.7	46.8	0.8
	CE2	B:TYQ382	3.8	34.6	0.8
	CG	B:HIS431	4.1	11.3	1.0
	ND1	B:HIS431	4.1	12.4	1.0
	NE2	B:HIS592	4.1	17.8	1.0
	ND1	B:HIS433	4.1	14.4	1.0
	OZ	B:TYQ382	4.2	26.3	0.2
	CE1	B:TYQ382	4.2	21.4	0.8
	CD2	B:HIS592	4.2	18.6	1.0
	CG	B:HIS433	4.2	13.8	1.0
	O	B:HOH817	4.2	17.8	1.0
	SD	B:MET602	4.9	27.8	1.0
	CA	B:HIS592	5.0	12.8	1.0
	CD2	B:TYQ382	5.0	27.2	0.8

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: Wed Jul 31 05:41:51 2024

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