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Copper in PDB 5uiz: Structure of T.Fusca AA10A

Protein crystallography data

The structure of Structure of T.Fusca AA10A, PDB code: 5uiz was solved by P.M.Alahuhta, V.V.Lunin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.78 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.228, 77.228, 122.346, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 22.9

Other elements in 5uiz:

The structure of Structure of T.Fusca AA10A also contains other interesting chemical elements:

Iodine (I) 28 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Structure of T.Fusca AA10A (pdb code 5uiz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of T.Fusca AA10A, PDB code: 5uiz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5uiz

Go back to Copper Binding Sites List in 5uiz
Copper binding site 1 out of 2 in the Structure of T.Fusca AA10A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of T.Fusca AA10A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:39.4
occ:0.50
ND1 A:HIS37 2.1 41.6 0.7
N A:HIS37 2.1 32.7 0.7
NE2 A:HIS144 2.2 33.5 1.0
CG A:HIS37 2.8 38.8 0.7
CE1 A:HIS37 3.0 43.1 0.7
CA A:HIS37 3.0 31.9 0.7
CD2 A:HIS144 3.1 31.4 1.0
CB A:HIS37 3.2 35.9 0.7
OH A:TYR213 3.2 30.2 1.0
CE1 A:HIS144 3.3 32.5 1.0
CD2 A:HIS37 3.9 42.8 0.7
NE2 A:HIS37 3.9 44.8 0.7
CB A:ALA142 4.0 26.8 1.0
OE1 A:GLN211 4.0 21.4 1.0
O A:HOH492 4.1 37.8 1.0
CG A:HIS144 4.3 31.9 1.0
C A:HIS37 4.3 28.6 0.7
ND1 A:HIS144 4.3 32.3 1.0
CZ A:TYR213 4.5 25.1 1.0
O A:HIS37 4.6 29.4 0.7
OD1 A:ASP140 4.7 28.3 1.0
NE2 A:HIS208 4.8 23.4 1.0

Copper binding site 2 out of 2 in 5uiz

Go back to Copper Binding Sites List in 5uiz
Copper binding site 2 out of 2 in the Structure of T.Fusca AA10A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of T.Fusca AA10A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu301

b:41.9
occ:0.31
ND1 B:HIS37 2.1 38.1 0.9
N B:HIS37 2.3 33.8 0.9
O B:HOH550 2.6 39.3 1.0
CE1 B:HIS37 3.0 40.0 0.9
CG B:HIS37 3.2 37.0 0.9
CE1 B:HIS144 3.2 29.3 1.0
CA B:HIS37 3.3 31.7 0.9
O B:HOH409 3.5 24.6 0.3
CB B:HIS37 3.6 34.0 0.9
OE1 B:GLN211 3.7 24.9 1.0
OH B:TYR213 3.8 21.4 1.0
ND1 B:HIS144 4.0 26.3 1.0
CB B:ALA142 4.0 24.6 1.0
NE2 B:HIS37 4.2 40.4 0.9
NE2 B:HIS144 4.2 28.3 1.0
CD2 B:HIS37 4.3 38.3 0.9
C B:HIS37 4.6 27.9 0.9
CD B:GLN211 4.7 22.7 1.0
O B:HIS37 4.9 27.6 0.9
NE2 B:GLN211 4.9 24.3 1.0

Reference:

N.Kruer-Zerhusen, M.Alahuhta, V.V.Lunin, M.E.Himmel, Y.J.Bomble, D.B.Wilson. Structure of A Thermobifida Fusca Lytic Polysaccharide Monooxygenase and Mutagenesis of Key Residues. Biotechnol Biofuels V. 10 243 2017.
ISSN: ESSN 1754-6834
PubMed: 29213309
DOI: 10.1186/S13068-017-0925-7
Page generated: Wed Jul 31 05:12:46 2024

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