Copper in PDB 3aws: Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low

Enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low

All present enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low, PDB code: 3aws was solved by Y.Matoba, M.Sugiyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.00 / 1.24
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	64.780, 97.360, 54.790, 90.00, 90.00, 90.00
*R / R_free (%)*	15.1 / 19.6

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low (pdb code 3aws). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low, PDB code: 3aws:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3aws

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Copper Binding Sites List in 3aws

Copper binding site 1 out of 3 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu500 b:25.2 occ:0.21	O	B:HOH617	1.6	22.7	1.0
	NE2	A:HIS194	2.2	13.2	1.0
	NE2	A:HIS190	2.2	12.4	1.0
	NE2	A:HIS216	2.2	18.2	1.0
	CE1	A:HIS216	3.0	17.4	1.0
	CE1	A:HIS194	3.1	11.1	1.0
	CE1	A:HIS190	3.1	11.1	1.0
	CD2	A:HIS194	3.2	11.8	1.0
	CD2	A:HIS190	3.2	11.0	1.0
	O	B:HOH509	3.3	24.5	0.9
	CD2	A:HIS216	3.4	16.5	1.0
	OH	B:TYR98	3.8	23.3	1.0
	CE2	A:PHE212	4.0	10.1	1.0
	ND1	A:HIS216	4.2	15.7	1.0
	ND1	A:HIS194	4.2	9.6	1.0
	ND1	A:HIS190	4.2	11.3	1.0
	CG	A:HIS194	4.2	10.4	1.0
	CZ	B:TYR98	4.3	16.5	1.0
	CE2	B:TYR98	4.3	16.9	1.0
	CG	A:HIS190	4.3	10.3	1.0
	CG	A:HIS216	4.4	13.0	1.0
	CD2	A:HIS215	4.6	15.2	1.0
	NE2	A:HIS63	4.7	9.7	1.0
	CE1	A:HIS38	4.7	12.1	1.0
	CZ	A:PHE212	4.7	10.2	1.0
	CD2	A:PHE212	4.7	9.1	1.0
	NE2	A:HIS215	4.7	16.5	1.0
	NE2	A:HIS38	4.8	11.6	1.0
	CE1	A:PHE59	4.9	9.2	1.0
	NE2	A:HIS54	4.9	16.1	0.4
	OG	A:SER206	4.9	11.2	1.0

Copper binding site 2 out of 3 in 3aws

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Copper Binding Sites List in 3aws

Copper binding site 2 out of 3 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu502 b:69.3 occ:0.50	O	A:HOH836	2.5	35.8	0.5
A:Cu502 b:69.3 occ:0.50	CG	A:PRO231	4.8	27.9	1.0

Copper binding site 3 out of 3 in 3aws

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Copper Binding Sites List in 3aws

Copper binding site 3 out of 3 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is Low within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cu501 b:21.4 occ:0.42	OE1	B:GLU67	1.7	47.6	1.0
	NE2	B:HIS82	2.0	21.8	1.0
	ND1	B:HIS68	2.0	50.6	1.0
	O	B:HIS68	2.1	49.8	1.0
	CE1	B:HIS68	2.7	50.9	1.0
	CD2	B:HIS82	2.8	22.4	1.0
	N	B:HIS68	2.8	47.0	1.0
	CD	B:GLU67	2.9	48.2	1.0
	C	B:HIS68	2.9	48.6	1.0
	CE1	B:HIS82	3.1	19.1	1.0
	CG	B:HIS68	3.2	50.0	1.0
	CA	B:HIS68	3.3	47.7	1.0
	C	B:GLU67	3.4	47.4	1.0
	CB	B:GLU67	3.6	50.5	1.0
	CB	B:HIS68	3.7	48.2	1.0
	OE2	B:GLU67	3.8	49.6	1.0
	CG	B:GLU67	3.8	49.7	1.0
	NE2	B:HIS68	3.9	51.0	1.0
	CG	B:HIS82	4.0	19.1	1.0
	ND1	B:HIS82	4.0	19.2	1.0
	CA	B:GLU67	4.1	49.1	1.0
	N	B:GLY69	4.1	47.8	1.0
	O	B:GLU67	4.1	49.5	1.0
	N	B:GLY70	4.1	47.6	1.0
	CD2	B:HIS68	4.2	50.6	1.0
	O	A:MET43	4.4	17.7	1.0
	CA	B:GLY69	4.6	47.1	1.0
	O	B:HOH640	4.7	25.2	1.0
	CA	B:GLY70	4.7	45.4	1.0
	C	B:GLY69	4.9	47.9	1.0

Reference:

Y.Matoba, N.Bando, K.Oda, M.Noda, F.Higashikawa, T.Kumagai, M.Sugiyama. A Molecular Mechanism For Copper Transportation to Tyrosinase That Is Assisted By A Metallochaperone, Caddie Protein J.Biol.Chem. V. 286 30219 2011.
ISSN: ISSN 0021-9258
PubMed: 21730070
DOI: 10.1074/JBC.M111.256818

Page generated: Mon Jul 14 01:55:10 2025

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