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Copper in PDB 5lm8: Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From From Aspergillus Niger

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

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

Protein crystallography data

The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From From Aspergillus Niger, PDB code: 5lm8 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) 29.44 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 200.709, 61.346, 53.836, 90.00, 95.29, 90.00
R / Rfree (%) 17.3 / 22.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From From Aspergillus Niger (pdb code 5lm8). 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 From Aspergillus Niger, PDB code: 5lm8:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 5lm8

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


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 From Aspergillus Niger within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:25.7
occ:0.75
ND1 A:HIS110 1.9 20.7 1.0
NE2 A:HIS152 2.0 29.4 1.0
NE2 A:HIS517 2.3 24.0 1.0
O2 A:PER618 2.4 36.0 1.0
CE1 A:HIS110 2.7 19.8 1.0
O1 A:PER618 2.9 24.3 1.0
CE1 A:HIS152 3.0 24.3 1.0
CD2 A:HIS152 3.0 23.6 1.0
CG A:HIS110 3.1 24.1 1.0
CD2 A:HIS517 3.2 26.6 1.0
CE1 A:HIS517 3.3 25.2 1.0
CB A:HIS110 3.6 21.9 1.0
NE2 A:HIS110 3.9 24.8 1.0
CZ2 A:TRP150 3.9 20.5 1.0
CU A:CU603 4.0 26.4 0.5
CD2 A:HIS110 4.1 21.1 1.0
CE2 A:TRP150 4.1 16.9 1.0
ND1 A:HIS152 4.1 20.0 1.0
NE1 A:TRP150 4.1 18.7 1.0
CG A:HIS152 4.2 20.7 1.0
CD2 A:HIS108 4.2 19.9 1.0
CD2 A:HIS451 4.3 21.4 1.0
NE2 A:HIS451 4.3 22.7 1.0
O A:HOH833 4.4 43.5 1.0
CG A:HIS517 4.4 24.7 1.0
ND1 A:HIS517 4.4 26.2 1.0
CA A:HIS110 4.6 21.9 1.0
CH2 A:TRP150 4.7 18.1 1.0
NE2 A:HIS108 4.8 21.9 1.0
CU A:CU602 5.0 32.2 1.0
CG A:HIS451 5.0 22.1 1.0

Copper binding site 2 out of 4 in 5lm8

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


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 From Aspergillus Niger within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:32.2
occ:1.00
NE2 A:HIS453 2.0 26.0 1.0
NE2 A:HIS515 2.1 21.1 1.0
NE2 A:HIS154 2.2 34.6 1.0
O1 A:PER618 2.4 24.3 1.0
O2 A:PER618 2.7 36.0 1.0
CE1 A:HIS453 2.7 24.7 1.0
CD2 A:HIS515 3.0 23.1 1.0
CD2 A:HIS154 3.1 25.9 1.0
CE1 A:HIS515 3.1 25.6 1.0
CD2 A:HIS453 3.1 24.8 1.0
CE1 A:HIS154 3.2 38.7 1.0
CD2 A:HIS451 3.4 21.4 1.0
CD2 A:LEU513 3.7 23.1 1.0
CU A:CU603 3.8 26.4 0.5
ND1 A:HIS453 3.9 25.3 1.0
CG A:HIS515 4.1 18.6 1.0
CG A:HIS453 4.1 24.1 1.0
O A:HOH833 4.2 43.5 1.0
NE2 A:HIS451 4.2 22.7 1.0
ND1 A:HIS515 4.2 24.7 1.0
CG A:HIS154 4.3 32.1 1.0
ND1 A:HIS154 4.3 33.8 1.0
CD2 A:HIS108 4.4 19.9 1.0
NE2 A:HIS108 4.5 21.9 1.0
CG A:HIS451 4.6 22.1 1.0
CB A:LEU513 4.6 21.1 1.0
CG A:LEU513 4.7 22.5 1.0
CU A:CU601 5.0 25.7 0.8

Copper binding site 3 out of 4 in 5lm8

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Copper binding site 3 out of 4 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From From Aspergillus Niger


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 From Aspergillus Niger within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:26.4
occ:0.50
NE2 A:HIS451 1.7 22.7 1.0
NE2 A:HIS108 2.0 21.9 1.0
O2 A:PER618 2.5 36.0 1.0
CD2 A:HIS451 2.6 21.4 1.0
CE1 A:HIS451 2.8 22.1 1.0
CD2 A:HIS108 2.8 19.9 1.0
O A:HOH849 3.0 22.3 1.0
CE1 A:HIS108 3.1 23.4 1.0
NE2 A:HIS453 3.1 26.0 1.0
CD2 A:HIS453 3.3 24.8 1.0
CE1 A:HIS453 3.6 24.7 1.0
ND1 A:HIS110 3.7 20.7 1.0
CG A:HIS451 3.7 22.1 1.0
ND1 A:HIS451 3.8 22.6 1.0
CA A:HIS110 3.8 21.9 1.0
CG A:HIS110 3.8 24.1 1.0
O1 A:PER618 3.8 24.3 1.0
CU A:CU602 3.8 32.2 1.0
CG A:HIS453 3.9 24.1 1.0
CG A:HIS108 4.0 20.0 1.0
ND1 A:HIS453 4.0 25.3 1.0
N A:GLY111 4.0 17.7 1.0
CU A:CU601 4.0 25.7 0.8
ND1 A:HIS108 4.0 23.2 1.0
CE1 A:HIS110 4.1 19.8 1.0
CB A:HIS110 4.2 21.9 1.0
CD2 A:HIS110 4.3 21.1 1.0
NE2 A:HIS110 4.4 24.8 1.0
C A:HIS110 4.5 17.9 1.0
CA A:HIS453 4.9 22.1 1.0
CB A:HIS453 4.9 19.8 1.0
N A:HIS110 4.9 22.5 1.0
O A:PHE109 4.9 20.7 1.0

Copper binding site 4 out of 4 in 5lm8

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


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 From Aspergillus Niger within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:22.1
occ:1.00
ND1 A:HIS521 2.0 17.8 1.0
ND1 A:HIS448 2.1 25.6 1.0
SG A:CYS516 2.2 19.7 1.0
CE1 A:HIS448 3.0 24.6 1.0
CE1 A:HIS521 3.0 20.3 1.0
CG A:HIS521 3.0 20.2 1.0
CG A:HIS448 3.1 24.3 1.0
CB A:CYS516 3.1 24.1 1.0
CB A:HIS521 3.3 22.1 1.0
CB A:HIS448 3.5 21.0 1.0
CD1 A:ILE518 3.5 21.8 1.0
CE2 A:PHE526 3.8 20.8 1.0
CD2 A:PHE526 3.8 21.3 1.0
CB A:ILE518 3.9 17.5 1.0
CG1 A:ILE518 4.0 18.8 1.0
NE2 A:HIS521 4.1 19.7 1.0
NE2 A:HIS448 4.1 23.7 1.0
CD2 A:HIS521 4.1 19.9 1.0
CD2 A:HIS448 4.2 20.4 1.0
CA A:HIS448 4.2 23.3 1.0
CA A:CYS516 4.5 22.5 1.0
CD A:PRO449 4.6 19.5 1.0
CZ A:PHE526 4.7 20.7 1.0
CG2 A:ILE518 4.7 17.5 1.0
CG A:PHE526 4.7 18.9 1.0
N A:ILE518 4.8 19.7 1.0
CA A:HIS521 4.9 23.0 1.0
O A:PRO447 4.9 25.1 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: Sun Dec 13 11:18:21 2020

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