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Sodium in PDB 8j6g: Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0

Enzymatic activity of Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0

All present enzymatic activity of Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0:
1.4.3.21;

Protein crystallography data

The structure of Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0, PDB code: 8j6g was solved by T.Murakawa, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.09
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.22, 62.144, 92.344, 90, 112.22, 90
R / Rfree (%) 19.8 / 22.5

Other elements in 8j6g:

The structure of Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0 also contains other interesting chemical elements:

Copper (Cu) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0 (pdb code 8j6g). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0, PDB code: 8j6g:

Sodium binding site 1 out of 1 in 8j6g

Go back to Sodium Binding Sites List in 8j6g
Sodium binding site 1 out of 1 in the Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Neutron Structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at Pd 9.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na702

b:8.7
occ:1.00
 OD1 A:ASP581 2.3 10.0 1.0
OD1 A:ASP440 2.3 8.9 1.0
O A:MET441 2.4 8.7 1.0
O A:ILE582 2.4 8.2 1.0
O A:HOH1161 2.7 9.8 1.0
H A:ILE582 2.7 8.7 0.0
D A:ILE582 2.8 7.7 1.0
D1 A:HOH1161 3.0 11.6 1.0
HD1 A:PHE446 3.1 13.0 1.0
D A:MET441 3.1 6.8 0.0
H A:MET441 3.1 5.3 1.0
N A:ILE582 3.2 8.3 1.0
DH22 A:ARG49 3.3 7.2 1.0
HH21 A:ARG49 3.3 11.1 0.2
D2 A:HOH1161 3.3 9.6 1.0
N A:MET441 3.3 7.6 1.0
C A:ILE582 3.4 7.7 1.0
C A:MET441 3.4 7.7 1.0
HA A:ASP581 3.5 8.8 1.0
CG A:ASP581 3.6 10.0 1.0
CG A:ASP440 3.6 8.7 1.0
C A:ASP581 3.7 8.5 1.0
HB2 A:MET441 3.7 7.4 1.0
C A:ASP440 3.8 7.3 1.0
HB2 A:TYR546 3.8 13.1 1.0
CA A:ILE582 3.9 8.1 1.0
CA A:MET441 3.9 7.6 1.0
HA A:ASP440 3.9 9.0 1.0
NH2 A:ARG49 4.0 10.8 1.0
DH21 A:ARG49 4.0 8.0 0.8
HE1 A:PHE446 4.0 14.2 1.0
CA A:ASP581 4.0 8.7 1.0
CD1 A:PHE446 4.0 12.8 1.0
HG23 A:VAL583 4.1 9.1 1.0
CA A:ASP440 4.3 7.7 1.0
CB A:ASP581 4.4 10.1 1.0
OD2 A:ASP440 4.4 9.3 1.0
CB A:MET441 4.4 8.4 1.0
HG13 A:ILE582 4.5 12.3 1.0
CE1 A:PHE446 4.5 13.8 1.0
O A:ASP440 4.5 8.3 1.0
HA A:ALA442 4.5 13.6 1.0
HG21 A:VAL583 4.5 10.1 1.0
HB1 A:ALA442 4.5 12.2 1.0
HA A:PHE446 4.5 12.0 1.0
OD2 A:ASP581 4.5 11.3 1.0
HA A:ILE582 4.5 9.2 1.0
HB3 A:ASN273 4.5 6.8 1.0
CB A:ASP440 4.5 8.2 1.0
HA A:VAL583 4.6 7.3 1.0
N A:VAL583 4.6 7.7 1.0
O A:ASP581 4.6 9.5 1.0
N A:ALA442 4.6 8.2 1.0
HG12 A:ILE582 4.6 10.6 1.0
HB3 A:PHE446 4.8 10.2 1.0
CB A:TYR546 4.8 10.9 1.0
CG2 A:VAL583 4.8 9.1 1.0
HB3 A:TYR546 4.8 9.3 1.0
HB2 A:ASN273 4.9 8.5 1.0
HA A:MET441 4.9 10.0 1.0
CG1 A:ILE582 4.9 10.0 1.0
O A:PHE446 4.9 11.6 1.0
OD1 A:ASN448 5.0 9.8 1.0

Reference:

T.Murakawa, K.Kurihara, M.Shoji, N.Yano, K.Kusaka, Y.Kawano, M.Suzuki, Y.Shigeta, T.Yano, M.Adachi, K.Tanizawa, T.Okajima. Neutron Crystallography of A Semiquinone Radical Intermediate of Copper Amine Oxidase Reveals A Substrate-Assisted Conformational Change of the Peptidyl Quinone Cofactor Acs Catalysis 12403 2023.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.3C02629
Page generated: Thu Dec 28 11:40:56 2023

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