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Copper in PDB 5opf: Structure of LPMO10B From From Micromonospora Aurantiaca

Protein crystallography data

The structure of Structure of LPMO10B From From Micromonospora Aurantiaca, PDB code: 5opf was solved by Z.Forsberg, B.Bissaro, J.Gullesen, B.Dalhus, G.Vaaje-Kolstad, V.G.H.Eijsink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.42 / 1.08
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.859, 55.088, 75.106, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 15.2

Copper Binding Sites:

The binding sites of Copper atom in the Structure of LPMO10B From From Micromonospora Aurantiaca (pdb code 5opf). 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 Structure of LPMO10B From From Micromonospora Aurantiaca, PDB code: 5opf:

Copper binding site 1 out of 1 in 5opf

Go back to Copper Binding Sites List in 5opf
Copper binding site 1 out of 1 in the Structure of LPMO10B From From Micromonospora Aurantiaca


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of LPMO10B From From Micromonospora Aurantiaca within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:7.5
occ:1.00
ND1 A:HIS37 2.0 8.1 1.0
NE2 A:HIS144 2.0 7.4 1.0
H1 A:HIS37 2.0 10.1 1.0
N A:HIS37 2.2 8.4 1.0
CE1 A:HIS144 2.9 7.0 1.0
CE1 A:HIS37 2.9 8.7 1.0
CG A:HIS37 3.0 7.6 1.0
H2 A:HIS37 3.0 10.1 1.0
OH A:TYR221 3.0 8.9 1.0
CD2 A:HIS144 3.0 7.0 1.0
HE1 A:HIS144 3.1 8.4 1.0
HE1 A:HIS37 3.2 10.4 1.0
CA A:HIS37 3.2 7.0 1.0
HD2 A:HIS144 3.2 8.4 1.0
HB2 A:HIS37 3.2 8.9 1.0
CB A:HIS37 3.3 7.4 1.0
HA A:HIS37 3.4 8.4 1.0
HB3 A:ALA142 3.5 9.3 1.0
HB2 A:ALA142 3.7 9.3 1.0
OE1 A:GLN219 3.9 9.2 1.0
CB A:ALA142 3.9 7.8 1.0
HE2 A:HIS216 4.0 10.3 1.0
HB1 A:ALA142 4.0 9.3 1.0
NE2 A:HIS37 4.1 8.7 1.0
ND1 A:HIS144 4.1 7.1 1.0
CD2 A:HIS37 4.1 8.6 1.0
CG A:HIS144 4.1 6.5 1.0
HE22 A:GLN219 4.2 13.1 1.0
HB3 A:HIS37 4.3 8.9 1.0
CZ A:TYR221 4.3 6.9 1.0
NE2 A:HIS216 4.4 8.6 1.0
C A:HIS37 4.5 7.3 1.0
HE1 A:HIS216 4.6 9.2 1.0
CD A:GLN219 4.7 8.7 1.0
NE2 A:GLN219 4.8 10.9 1.0
HH2 A:TRP212 4.8 8.3 1.0
CE1 A:HIS216 4.8 7.6 1.0
HE2 A:HIS37 4.8 10.4 1.0
HD1 A:HIS144 4.8 8.5 1.0
HE2 A:TYR221 4.9 9.9 1.0
HD2 A:HIS37 4.9 10.4 1.0
O A:HIS37 4.9 9.9 1.0

Reference:

Z.Forsberg, B.Bissaro, J.Gullesen, B.Dalhus, G.Vaaje-Kolstad, V.G.H.Eijsink. Structural Determinants of Bacterial Lytic Polysaccharide Monooxygenase Functionality. J. Biol. Chem. V. 293 1397 2018.
ISSN: ESSN 1083-351X
PubMed: 29222333
DOI: 10.1074/JBC.M117.817130
Page generated: Sun Dec 13 11:19:34 2020

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