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

Go back to

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy