Copper in PDB 1avl: Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone

Enzymatic activity of Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone

All present enzymatic activity of Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone, PDB code: 1avl was solved by M.C.J.Wilce, J.M.Guss, H.C.Freeman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 2.80
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	158.200, 64.100, 92.900, 90.00, 112.70, 90.00
*R / R_free (%)*	15 / 20.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone (pdb code 1avl). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone, PDB code: 1avl:

Copper binding site 1 out of 1 in 1avl

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Copper Binding Sites List in 1avl

Copper binding site 1 out of 1 in the Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu639 b:38.0 occ:1.00	NE2	A:HIS431	2.0	2.0	1.0
	NE2	A:HIS433	2.1	34.1	1.0
	ND1	A:HIS592	2.3	31.7	0.6
	O4	A:TPQ382	2.4	25.8	1.0
	CE1	A:HIS431	2.9	12.8	1.0
	CD2	A:HIS431	3.0	10.4	1.0
	CD2	A:HIS433	3.1	33.3	1.0
	CE1	A:HIS433	3.1	31.6	1.0
	ND1	A:HIS592	3.1	31.4	0.4
	CE1	A:HIS592	3.2	26.8	0.6
	C4	A:TPQ382	3.2	45.9	1.0
	CG	A:HIS592	3.3	28.5	0.6
	CB	A:HIS592	3.5	29.1	1.0
	O5	A:TPQ382	3.6	47.9	1.0
	CG	A:HIS592	3.8	33.8	0.4
	C5	A:TPQ382	3.8	46.2	1.0
	ND1	A:HIS431	4.1	10.0	1.0
	CG	A:HIS431	4.1	9.5	1.0
	C3	A:TPQ382	4.1	45.1	1.0
	CE1	A:HIS592	4.2	29.6	0.4
	ND1	A:HIS433	4.2	25.3	1.0
	CG	A:HIS433	4.2	28.4	1.0
	NE2	A:HIS592	4.3	30.1	0.6
	CD2	A:HIS592	4.4	31.9	0.6
	SD	A:MET602	4.4	35.8	1.0
	CE	A:MET602	4.6	30.6	1.0
	C6	A:TPQ382	5.0	41.6	1.0
	CD2	A:HIS592	5.0	38.6	0.4

Reference:

M.C.Wilce, D.M.Dooley, H.C.Freeman, J.M.Guss, H.Matsunami, W.S.Mcintire, C.E.Ruggiero, K.Tanizawa, H.Yamaguchi. Crystal Structures of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis in the Holo and Apo Forms: Implications For the Biogenesis of Topaquinone. Biochemistry V. 36 16116 1997.
ISSN: ISSN 0006-2960
PubMed: 9405045
DOI: 10.1021/BI971797I

Page generated: Tue Jul 30 21:35:34 2024

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