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Copper in PDB 6haq: AFGH61B Wild-Type Copper Loaded

Protein crystallography data

The structure of AFGH61B Wild-Type Copper Loaded, PDB code: 6haq was solved by L.Lo Leggio, J.C.N.Poulsen, C.D.Weihe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.65 / 1.37
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 44.300, 49.110, 53.960, 75.86, 88.38, 76.31
R / Rfree (%) 10.5 / 15.6

Copper Binding Sites:

The binding sites of Copper atom in the AFGH61B Wild-Type Copper Loaded (pdb code 6haq). 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 Wild-Type Copper Loaded, PDB code: 6haq:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6haq

Go back to Copper Binding Sites List in 6haq
Copper binding site 1 out of 2 in the AFGH61B Wild-Type Copper Loaded


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of AFGH61B Wild-Type Copper Loaded within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:15.3
occ:0.80
ND1 A:HIC1 1.9 15.6 1.0
NE2 A:HIS86 2.0 15.2 1.0
N A:HIC1 2.2 18.9 1.0
O A:HOH484 2.4 34.7 1.0
OH A:TYR175 2.8 13.1 1.0
O A:HOH679 2.9 43.5 1.0
CG A:HIC1 2.9 17.8 1.0
CD2 A:HIS86 3.0 16.1 1.0
CE1 A:HIS86 3.0 19.0 1.0
CE1 A:HIC1 3.0 17.5 1.0
CA A:HIC1 3.1 14.7 1.0
CB A:HIC1 3.4 15.7 1.0
O A:HOH724 3.8 49.2 1.0
OE1 A:GLN173 3.9 16.8 1.0
CZ A:TYR175 3.9 11.0 1.0
NE2 A:HIC1 4.1 19.9 1.0
ND1 A:HIS86 4.1 16.8 1.0
CG A:HIS86 4.1 15.3 1.0
CD2 A:HIC1 4.1 18.6 1.0
O A:HOH689 4.4 38.8 1.0
C A:HIC1 4.5 15.2 1.0
CE2 A:TYR175 4.5 12.4 1.0
CG A:PRO83 4.6 22.7 1.0
O A:HIC1 4.9 18.5 1.0
CE1 A:TYR175 5.0 12.8 1.0
CD A:GLN173 5.0 15.8 1.0

Copper binding site 2 out of 2 in 6haq

Go back to Copper Binding Sites List in 6haq
Copper binding site 2 out of 2 in the AFGH61B Wild-Type Copper Loaded


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of AFGH61B Wild-Type Copper Loaded within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu301

b:13.2
occ:0.85
ND1 B:HIC1 1.9 14.4 1.0
NE2 B:HIS86 2.0 13.7 1.0
O B:HOH430 2.0 28.3 1.0
N B:HIC1 2.2 15.3 1.0
O B:HOH656 2.6 28.4 1.0
OH B:TYR175 2.8 13.3 1.0
CE1 B:HIC1 2.9 16.9 1.0
CG B:HIC1 2.9 15.1 1.0
CD2 B:HIS86 2.9 13.7 1.0
CE1 B:HIS86 3.0 12.8 1.0
CA B:HIC1 3.2 13.3 1.0
CB B:HIC1 3.3 13.8 1.0
OE1 B:GLN173 3.8 14.0 1.0
CZ B:TYR175 3.9 10.9 1.0
NE2 B:HIC1 4.1 18.6 1.0
CD2 B:HIC1 4.1 16.8 1.0
CG B:HIS86 4.1 12.4 1.0
ND1 B:HIS86 4.1 11.8 1.0
O B:HOH776 4.4 80.3 1.0
CE2 B:TYR175 4.4 11.7 1.0
C B:HIC1 4.5 13.8 1.0
CG B:PRO83 4.6 17.1 1.0
O B:HOH581 4.9 18.9 1.0
CE1 B:TYR175 4.9 11.3 1.0
O B:HIC1 4.9 16.7 1.0
CD B:GLN173 4.9 12.5 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 11:22:50 2020

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