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Copper in PDB 7wno: Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data.

Enzymatic activity of Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data.

All present enzymatic activity of Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data.:
1.4.3.21;

Copper Binding Sites:

The binding sites of Copper atom in the Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data. (pdb code 7wno). 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 Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data., PDB code: 7wno:

Copper binding site 1 out of 1 in 7wno

Go back to Copper Binding Sites List in 7wno
Copper binding site 1 out of 1 in the Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystallographic Structure of Copper Amine Oxidase From Arthrobacter Glibiformis at Pd 7.4 Determined By Only Neutron Diffraction Data. within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Cu701

b:13.1
occ:1.00
NE2 X:HIS433 1.9 12.4 1.0
NE2 X:HIS431 1.9 9.7 1.0
ND1 X:HIS592 2.0 12.5 1.0
D2 X:DOD1208 2.2 14.9 1.0
O X:DOD1208 2.4 17.4 1.0
D1 X:DOD1208 2.5 14.7 1.0
D2 X:DOD1250 2.5 24.6 1.0
O X:DOD1250 2.6 17.2 1.0
D1 X:DOD1250 2.9 18.7 1.0
CD2 X:HIS433 2.9 15.2 1.0
CE1 X:HIS433 2.9 10.8 1.0
CD2 X:HIS431 2.9 12.5 1.0
CE1 X:HIS431 2.9 11.4 1.0
CE1 X:HIS592 3.0 8.9 1.0
CG X:HIS592 3.0 20.3 1.0
HD2 X:HIS431 3.1 9.6 1.0
HD2 X:HIS433 3.1 11.0 1.0
HE1 X:HIS433 3.1 18.7 1.0
HB3 X:HIS592 3.2 7.5 1.0
HE1 X:HIS431 3.2 10.2 1.0
HE1 X:HIS592 3.3 20.4 1.0
HB2 X:HIS592 3.3 8.0 1.0
CB X:HIS592 3.4 10.5 1.0
D1 X:DOD1394 3.5 40.1 1.0
O X:DOD1195 3.9 10.1 1.0
ND1 X:HIS433 4.0 13.9 1.0
CG X:HIS433 4.0 8.9 1.0
ND1 X:HIS431 4.0 11.8 1.0
CG X:HIS431 4.0 8.8 1.0
O X:DOD1394 4.0 34.3 1.0
NE2 X:HIS592 4.1 13.5 1.0
CD2 X:HIS592 4.2 13.7 1.0
HE1 X:MET602 4.3 26.4 1.0
D1 X:DOD1195 4.3 23.6 1.0
D2 X:DOD1394 4.4 14.9 1.0
D2 X:DOD905 4.4 10.3 1.0
D1 X:DOD905 4.5 11.8 1.0
HG13 X:VAL406 4.5 14.5 0.2
D1 X:DOD832 4.6 40.0 1.0
HG12 X:VAL406 4.6 9.9 0.8
D3 X:TPQ382 4.6 24.9 1.0
D2 X:DOD1195 4.7 23.8 1.0
O X:DOD905 4.7 25.5 1.0
O2 X:TPQ382 4.8 17.7 1.0
DD1 X:HIS433 4.9 5.4 1.0
CA X:HIS592 4.9 13.3 1.0
SD X:MET602 4.9 26.3 1.0
HG3 X:PRO594 4.9 16.1 1.0
HB1 X:ALA402 5.0 18.9 1.0

Reference:

T.Murakawa, K.Kurihara, M.Adachi, K.Kusaka, K.Tanizawa, T.Okajima. Re-Evaluation of Protein Neutron Crystallography with and Without X-Ray/Neutron Joint Refinement. Iucrj V. 9 342 2022.
ISSN: ESSN 2052-2525
PubMed: 35546796
DOI: 10.1107/S2052252522003657
Page generated: Wed Jul 31 09:21:11 2024

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