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Copper in PDB 2yx9: Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis

Enzymatic activity of Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2yx9 was solved by T.Murakawa, T.Okajima, H.Yamaguchi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.88 / 1.68
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.012, 63.027, 184.119, 90.00, 111.96, 90.00
R / Rfree (%) 24.5 / 25.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis (pdb code 2yx9). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2yx9:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2yx9

Go back to Copper Binding Sites List in 2yx9
Copper binding site 1 out of 2 in the Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis


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 D298K Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:25.2
occ:1.00
NE2 A:HIS431 2.1 19.7 1.0
NE2 A:HIS433 2.1 24.6 1.0
ND1 A:HIS592 2.2 24.7 1.0
O A:HOH1351 2.5 37.7 1.0
CD2 A:HIS433 3.0 24.2 1.0
CD2 A:HIS431 3.0 18.2 1.0
CE1 A:HIS431 3.1 21.5 1.0
CG A:HIS592 3.1 22.9 1.0
CE1 A:HIS592 3.2 25.6 1.0
CE1 A:HIS433 3.2 26.3 1.0
CB A:HIS592 3.3 20.3 1.0
O A:HOH1361 3.5 45.9 1.0
ND1 A:HIS431 4.1 17.4 1.0
CG A:HIS431 4.2 17.5 1.0
CG A:HIS433 4.2 22.9 1.0
ND1 A:HIS433 4.2 25.1 1.0
CD2 A:HIS592 4.3 23.9 1.0
NE2 A:HIS592 4.3 22.7 1.0
O A:HOH1196 4.3 40.4 1.0
O A:HOH1081 4.4 25.5 1.0
CA A:HIS592 4.8 18.8 1.0
SD A:MET602 4.9 34.8 1.0

Copper binding site 2 out of 2 in 2yx9

Go back to Copper Binding Sites List in 2yx9
Copper binding site 2 out of 2 in the Crystal Structure of D298K Copper Amine Oxidase From Arthrobacter Globiformis


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 D298K Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1002

b:25.5
occ:1.00
NE2 B:HIS431 2.1 20.0 1.0
NE2 B:HIS433 2.2 25.1 1.0
ND1 B:HIS592 2.2 23.1 1.0
O B:HOH1408 2.6 36.9 1.0
CD2 B:HIS433 2.9 26.5 1.0
CE1 B:HIS431 3.0 20.8 1.0
CD2 B:HIS431 3.1 20.0 1.0
CG B:HIS592 3.1 22.6 1.0
CE1 B:HIS592 3.2 24.2 1.0
CE1 B:HIS433 3.3 26.9 1.0
CB B:HIS592 3.3 20.0 1.0
ND1 B:HIS431 4.1 18.5 1.0
CG B:HIS433 4.2 23.0 1.0
CG B:HIS431 4.2 18.3 1.0
CD2 B:HIS592 4.2 22.7 1.0
NE2 B:HIS592 4.3 23.1 1.0
ND1 B:HIS433 4.3 25.6 1.0
O B:HOH1307 4.4 43.5 1.0
O B:HOH1103 4.5 25.1 1.0
SD B:MET602 4.8 35.2 1.0
CA B:HIS592 4.8 19.0 1.0

Reference:

R.H.Moore, M.A.Spies, M.B.Culpepper, T.Murakawa, S.Hirota, T.Okajima, K.Tanizawa, M.Mure. Trapping of A Dopaquinone Intermediate in the Tpq Cofactor Biogenesis in A Copper-Containing Amine Oxidase From Arthrobacter Globiformis. J.Am.Chem.Soc. V. 129 11524 2007.
ISSN: ISSN 0002-7863
PubMed: 17715921
DOI: 10.1021/JA0731165
Page generated: Wed Oct 28 14:22:46 2020
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