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Copper in PDB 6ha5: AFGH61B L90V/D131S/M134L/A141W Variant

Protein crystallography data

The structure of AFGH61B L90V/D131S/M134L/A141W Variant, PDB code: 6ha5 was solved by L.Lo Leggio, J.C.N.Poulsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.37 / 1.87
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 38.100, 44.280, 60.000, 89.64, 108.32, 108.95
R / Rfree (%) 13.9 / 18.2

Copper Binding Sites:

The binding sites of Copper atom in the AFGH61B L90V/D131S/M134L/A141W Variant (pdb code 6ha5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the AFGH61B L90V/D131S/M134L/A141W Variant, PDB code: 6ha5:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6ha5

Go back to Copper Binding Sites List in 6ha5
Copper binding site 1 out of 2 in the AFGH61B L90V/D131S/M134L/A141W Variant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of AFGH61B L90V/D131S/M134L/A141W Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:19.7
occ:0.40
ND1 A:HIC1 1.8 35.0 1.0
NE2 A:HIS86 2.1 16.4 1.0
N A:HIC1 2.4 30.1 1.0
CG A:HIC1 2.7 34.6 1.0
CD2 A:HIS86 2.9 18.7 1.0
CE1 A:HIC1 2.9 35.6 1.0
OH A:TYR175 3.0 16.4 1.0
CB A:HIC1 3.1 33.4 1.0
CE1 A:HIS86 3.1 18.2 1.0
CA A:HIC1 3.2 29.5 1.0
CD2 A:HIC1 3.9 36.1 1.0
NE2 A:HIC1 4.0 37.2 1.0
CZ A:TYR175 4.0 14.6 1.0
OE1 A:GLN173 4.0 17.8 1.0
CG A:HIS86 4.1 17.0 1.0
ND1 A:HIS86 4.1 16.3 1.0
CE2 A:TYR175 4.5 14.8 1.0
C A:HIC1 4.6 26.4 1.0
CG A:PRO83 4.6 19.7 1.0
O A:HIC1 5.0 27.0 1.0

Copper binding site 2 out of 2 in 6ha5

Go back to Copper Binding Sites List in 6ha5
Copper binding site 2 out of 2 in the AFGH61B L90V/D131S/M134L/A141W Variant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of AFGH61B L90V/D131S/M134L/A141W Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu301

b:30.1
occ:0.30
ND1 B:HIC1 1.9 51.0 1.0
NE2 B:HIS86 2.2 32.1 1.0
N B:HIC1 2.5 41.4 1.0
CG B:HIC1 2.8 48.3 1.0
O B:HOH552 2.9 37.1 1.0
CD2 B:HIS86 3.0 30.4 1.0
CE1 B:HIC1 3.0 56.1 1.0
OH B:TYR175 3.1 27.8 1.0
CB B:HIC1 3.1 44.0 1.0
CE1 B:HIS86 3.2 29.9 1.0
CA B:HIC1 3.3 40.6 1.0
OE1 B:GLN173 3.9 27.7 1.0
CD2 B:HIC1 4.0 52.5 1.0
NE2 B:HIC1 4.1 56.0 1.0
CG B:HIS86 4.1 31.2 1.0
ND1 B:HIS86 4.2 30.6 1.0
CZ B:TYR175 4.2 26.7 1.0
CG B:PRO83 4.6 32.5 1.0
C B:HIC1 4.7 33.4 1.0
CE2 B:TYR175 4.8 24.6 1.0
CD B:GLN173 5.0 29.4 1.0

Reference:

L.Lo Leggio, C.D.Weihe, J.N.Poulsen, M.Sweeney, F.Rasmussen, J.Lin, L.De Maria, M.Wogulis. Structure of A Lytic Polysaccharide Monooxygenase From Aspergillus Fumigatus and An Engineered Thermostable Variant. Carbohydr. Res. V. 469 55 2018.
ISSN: ISSN 1873-426X
PubMed: 30296642
DOI: 10.1016/J.CARRES.2018.08.009
Page generated: Sun Dec 13 11:22:49 2020

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