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Copper in PDB 5tki: Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement

Protein crystallography data

The structure of Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement, PDB code: 5tki was solved by W.B.O'dell, F.Meilleur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.120, 42.230, 70.290, 90.00, 98.33, 90.00
R / Rfree (%) 21.6 / 25.3

Copper Binding Sites:

The binding sites of Copper atom in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement (pdb code 5tki). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement, PDB code: 5tki:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5tki

Go back to Copper Binding Sites List in 5tki
Copper binding site 1 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:14.9
occ:1.00
NE2 A:HIS84 2.0 10.2 1.0
ND1 A:HIS1 2.0 11.1 1.0
O B:HOH411 2.0 15.1 1.0
N A:HIS1 2.1 11.3 1.0
D2 A:HIS1 2.4 13.6 1.0
D1 B:HOH411 2.4 18.1 1.0
O A:HOH558 2.4 18.5 1.0
D3 A:HIS1 2.5 13.6 1.0
D2 B:HOH411 2.6 18.1 1.0
D2 A:HOH558 2.7 22.2 1.0
OH A:TYR168 2.7 13.9 1.0
CE1 A:HIS84 2.9 13.2 1.0
DH A:TYR168 2.9 16.7 1.0
CE1 A:HIS1 3.0 12.8 1.0
HE1 A:HIS84 3.0 15.9 1.0
CG A:HIS1 3.0 14.0 1.0
CD2 A:HIS84 3.1 11.5 1.0
CA A:HIS1 3.1 9.8 1.0
D1 A:HOH558 3.1 22.2 1.0
HE1 A:HIS1 3.2 15.4 1.0
HD2 A:HIS84 3.3 13.8 1.0
HA A:HIS1 3.3 11.8 1.0
CB A:HIS1 3.4 12.7 1.0
HB2 A:HIS1 3.4 15.3 1.0
D2 A:HOH486 3.6 22.1 1.0
CZ A:TYR168 3.7 11.7 1.0
OE1 A:GLN166 3.7 13.7 1.0
ND1 A:HIS84 4.0 14.6 1.0
NE2 A:HIS1 4.1 16.2 1.0
OE1 B:GLU30 4.1 23.9 1.0
HE1 A:TYR168 4.1 12.7 1.0
CD2 A:HIS1 4.1 14.2 1.0
CG A:HIS84 4.1 14.9 1.0
D1 B:HOH447 4.2 35.8 1.0
O B:HOH447 4.2 29.8 1.0
O A:HOH486 4.2 18.4 1.0
D1 A:HOH486 4.2 22.1 1.0
HB3 A:HIS1 4.3 15.3 1.0
CE1 A:TYR168 4.3 10.6 1.0
HD3 A:PRO28 4.3 16.4 1.0
D2 B:HOH447 4.4 35.8 1.0
C A:HIS1 4.4 10.8 1.0
CE2 A:TYR168 4.6 10.9 1.0
HE2 A:TYR168 4.7 13.1 1.0
HE1 A:HIS157 4.7 16.2 1.0
HG3 A:MET80 4.8 15.8 1.0
DD1 A:HIS84 4.8 17.5 1.0
CD A:GLN166 4.8 14.6 1.0
D1 A:HOH571 4.8 35.8 1.0
DE2 A:HIS1 4.8 19.4 1.0
O A:HIS1 4.9 13.1 1.0
HG3 A:PRO28 4.9 17.6 1.0
HD2 A:HIS1 5.0 17.1 1.0
O A:HOH571 5.0 29.9 1.0
D2 A:HOH506 5.0 32.4 1.0

Copper binding site 2 out of 2 in 5tki

Go back to Copper Binding Sites List in 5tki
Copper binding site 2 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu303

b:17.0
occ:1.00
O A:HOH419 1.9 14.1 1.0
ND1 B:HIS1 2.0 16.1 1.0
NE2 B:HIS84 2.0 18.0 1.0
N B:HIS1 2.0 10.3 1.0
D2 A:HOH419 2.4 17.0 1.0
DH B:TYR168 2.4 18.0 1.0
D3 B:HIS1 2.4 12.4 1.0
O B:HOH534 2.5 18.4 1.0
D1 A:HOH419 2.5 17.0 1.0
D2 B:HIS1 2.6 12.4 1.0
OH B:TYR168 2.7 15.0 1.0
D2 B:HOH534 2.8 22.1 1.0
D1 B:HOH534 2.9 22.1 1.0
CE1 B:HIS84 2.9 16.4 1.0
CG B:HIS1 3.0 11.4 1.0
CE1 B:HIS1 3.0 16.5 1.0
HE1 B:HIS84 3.0 19.7 1.0
CD2 B:HIS84 3.1 12.6 1.0
CA B:HIS1 3.1 11.5 1.0
HE1 B:HIS1 3.2 19.8 1.0
HD2 B:HIS84 3.3 15.1 1.0
CB B:HIS1 3.3 14.3 1.0
HA B:HIS1 3.4 13.8 1.0
HB2 B:HIS1 3.4 17.2 1.0
D1 A:HOH406 3.7 42.4 1.0
D2 B:HOH449 3.7 25.4 1.0
OE1 B:GLN166 3.7 16.4 1.0
CZ B:TYR168 3.7 14.7 1.0
ND1 B:HIS84 4.1 17.0 1.0
NE2 B:HIS1 4.1 15.1 1.0
CD2 B:HIS1 4.1 15.0 1.0
OE2 A:GLU30 4.1 34.4 0.6
OE1 A:GLU30 4.2 33.3 0.4
D2 A:HOH406 4.2 42.4 1.0
CG B:HIS84 4.2 14.9 1.0
O B:HOH449 4.2 21.1 1.0
HE1 B:TYR168 4.2 15.1 1.0
HB3 B:HIS1 4.3 17.2 1.0
O A:HOH406 4.3 35.3 1.0
HD3 B:PRO28 4.4 18.5 1.0
CE1 B:TYR168 4.4 12.6 1.0
C B:HIS1 4.4 18.0 1.0
HE1 B:HIS157 4.5 23.0 1.0
HE2 B:TYR168 4.6 15.4 1.0
D1 B:HOH449 4.6 25.4 1.0
CE2 B:TYR168 4.6 12.9 1.0
HG3 B:MET80 4.8 23.9 1.0
CD B:GLN166 4.8 15.1 1.0
DD1 B:HIS84 4.8 20.4 1.0
DE2 B:HIS1 4.9 18.1 1.0
O B:HIS1 4.9 14.5 1.0
HD2 B:HIS1 5.0 18.0 1.0

Reference:

W.B.O'dell, P.K.Agarwal, F.Meilleur. Oxygen Activation at the Active Site of A Fungal Lytic Polysaccharide Monooxygenase. Angew. Chem. Int. Ed. Engl. V. 56 767 2017.
ISSN: ESSN 1521-3773
PubMed: 28004877
DOI: 10.1002/ANIE.201610502
Page generated: Sun Dec 13 11:19:44 2020

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