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Copper in PDB 5lww: Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc

Enzymatic activity of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc

All present enzymatic activity of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc, PDB code: 5lww was solved by M.Ferraroni, F.Briganti, J.A.Tamayo-Ramos, W.J.H.Van Berkel, A.H.Westphal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.65
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 88.446, 128.158, 134.676, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 26.7

Other elements in 5lww:

The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc also contains other interesting chemical elements:

Potassium (K) 1 atom
Zinc (Zn) 8 atoms
Chlorine (Cl) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc (pdb code 5lww). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc, PDB code: 5lww:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 5lww

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Copper binding site 1 out of 4 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu612

b:44.7
occ:1.00
 ND1 A:HIS110 1.9 36.0 1.0
NE2 A:HIS152 2.1 29.2 1.0
NE2 A:HIS517 2.1 35.3 1.0
O A:HOH870 2.4 15.2 1.0
CE1 A:HIS152 2.8 30.5 1.0
CE1 A:HIS110 2.8 33.0 1.0
CG A:HIS110 3.0 33.6 1.0
CE1 A:HIS517 3.1 37.2 1.0
CD2 A:HIS517 3.1 39.9 1.0
CD2 A:HIS152 3.3 30.9 1.0
CB A:HIS110 3.5 30.6 1.0
NE2 A:HIS110 4.0 34.5 1.0
ND1 A:HIS152 4.0 30.6 1.0
CU A:CU614 4.1 57.5 1.0
CD2 A:HIS110 4.1 33.1 1.0
O A:HOH878 4.1 57.8 1.0
CD2 A:HIS451 4.1 35.8 1.0
CZ2 A:TRP150 4.1 34.2 1.0
ND1 A:HIS517 4.2 42.7 1.0
NE2 A:HIS451 4.2 36.3 1.0
CG A:HIS517 4.2 42.5 1.0
CD2 A:HIS108 4.3 28.5 1.0
CG A:HIS152 4.3 33.3 1.0
CE2 A:TRP150 4.4 34.1 1.0
CU A:CU613 4.4 42.1 1.0
NE1 A:TRP150 4.4 32.1 1.0
CA A:HIS110 4.6 30.7 1.0
NE2 A:HIS108 4.8 28.0 1.0
CH2 A:TRP150 4.8 34.1 1.0

Copper binding site 2 out of 4 in 5lww

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Copper binding site 2 out of 4 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu613

b:42.1
occ:1.00
 NE2 A:HIS154 2.0 36.0 1.0
O A:HOH870 2.0 15.2 1.0
NE2 A:HIS453 2.2 34.2 1.0
NE2 A:HIS515 2.2 35.3 1.0
CD2 A:HIS154 3.0 37.1 1.0
CE1 A:HIS154 3.0 38.4 1.0
CE1 A:HIS453 3.0 33.0 1.0
CE1 A:HIS515 3.1 34.8 1.0
CD2 A:HIS515 3.1 36.0 1.0
CD2 A:HIS453 3.3 31.6 1.0
CD2 A:HIS451 3.6 35.8 1.0
CU A:CU614 3.8 57.5 1.0
O A:HOH878 4.0 57.8 1.0
ND1 A:HIS154 4.1 35.0 1.0
CG A:HIS154 4.1 34.1 1.0
ND1 A:HIS515 4.1 34.6 1.0
NE2 A:HIS451 4.2 36.3 1.0
CG A:HIS515 4.2 34.8 1.0
ND1 A:HIS453 4.2 34.5 1.0
CD2 A:HIS108 4.2 28.5 1.0
CD2 A:LEU513 4.3 29.5 1.0
NE2 A:HIS108 4.3 28.0 1.0
CG A:HIS453 4.3 34.1 1.0
CU A:CU612 4.4 44.7 1.0
CG A:HIS451 4.7 33.3 1.0
CD2 A:HIS517 4.8 39.9 1.0
CE1 A:HIS152 4.8 30.5 1.0
CG A:HIS108 4.9 29.9 1.0
NE2 A:HIS517 4.9 35.3 1.0

Copper binding site 3 out of 4 in 5lww

Go back to Copper Binding Sites List in 5lww
Copper binding site 3 out of 4 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu614

b:57.5
occ:1.00
 NE2 A:HIS108 1.9 28.0 1.0
NE2 A:HIS451 1.9 36.3 1.0
O A:HOH831 2.6 39.9 1.0
CD2 A:HIS108 2.8 28.5 1.0
CD2 A:HIS451 2.9 35.8 1.0
CE1 A:HIS108 2.9 27.6 1.0
CE1 A:HIS451 3.0 34.9 1.0
NE2 A:HIS453 3.3 34.2 1.0
O A:HOH870 3.4 15.2 1.0
CE1 A:HIS453 3.5 33.0 1.0
ND1 A:HIS110 3.5 36.0 1.0
CD2 A:HIS453 3.5 31.6 1.0
CG A:HIS110 3.7 33.6 1.0
CA A:HIS110 3.7 30.7 1.0
CU A:CU613 3.8 42.1 1.0
ND1 A:HIS453 3.8 34.5 1.0
CG A:HIS453 3.8 34.1 1.0
CG A:HIS108 4.0 29.9 1.0
ND1 A:HIS108 4.0 31.2 1.0
CB A:HIS110 4.0 30.6 1.0
CG A:HIS451 4.0 33.3 1.0
ND1 A:HIS451 4.0 32.9 1.0
CE1 A:HIS110 4.1 33.0 1.0
N A:GLY111 4.1 31.3 1.0
CU A:CU612 4.1 44.7 1.0
CD2 A:HIS110 4.3 33.1 1.0
C A:HIS110 4.4 31.4 1.0
NE2 A:HIS110 4.5 34.5 1.0
O A:HOH709 4.6 35.4 1.0
CA A:HIS453 4.6 31.2 1.0
N A:HIS110 4.6 29.1 1.0
CB A:HIS453 4.8 32.9 1.0
O A:PHE109 4.9 30.3 1.0
O A:HOH769 5.0 33.7 1.0

Copper binding site 4 out of 4 in 5lww

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Copper binding site 4 out of 4 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu615

b:42.7
occ:1.00
 ND1 A:HIS521 2.0 31.9 1.0
SG A:CYS516 2.2 38.7 1.0
ND1 A:HIS448 2.2 42.3 1.0
CE1 A:HIS521 2.9 31.6 1.0
CG A:HIS521 3.0 32.8 1.0
CG A:HIS448 3.0 38.7 1.0
CE1 A:HIS448 3.1 40.3 1.0
CB A:CYS516 3.3 35.4 1.0
CB A:HIS448 3.3 38.8 1.0
CD1 A:ILE518 3.4 26.5 1.0
CB A:HIS521 3.4 33.4 1.0
CE2 A:PHE526 3.7 32.5 1.0
CD2 A:PHE526 3.7 30.7 1.0
CB A:ILE518 3.8 31.1 1.0
CG1 A:ILE518 3.9 28.2 1.0
NE2 A:HIS521 4.0 29.7 1.0
CD2 A:HIS448 4.1 38.3 1.0
CD2 A:HIS521 4.1 31.1 1.0
NE2 A:HIS448 4.1 38.1 1.0
CA A:HIS448 4.2 47.5 1.0
CG2 A:ILE518 4.5 29.0 1.0
CA A:CYS516 4.6 37.8 1.0
CG A:PHE526 4.6 28.9 1.0
CZ A:PHE526 4.6 27.6 1.0
N A:ILE518 4.8 41.1 1.0
CD A:PRO449 4.8 40.8 1.0
CA A:ILE518 4.9 37.1 1.0
O A:HOH823 4.9 34.1 1.0
O A:PRO447 4.9 40.6 1.0
CA A:HIS521 4.9 34.6 1.0

Reference:

M.Ferraroni, A.H.Westphal, M.Borsari, J.A.Tamayo-Ramos, F.Briganti, L.H.De Graaff, W.J.H.Van Berkel. Structure and Function of Aspergillus Niger Laccase Mcog Biocatalysis 2017.
ISSN: ESSN 2353-1746
DOI: 10.1515/BOCA-2017-0001
Page generated: Mon Jul 14 04:51:46 2025

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