Atomistry » Copper » PDB 5i26-5luf » 5lm8
Atomistry »
  Copper »
    PDB 5i26-5luf »
      5lm8 »

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

Go back to Copper Binding Sites List in 5lm8
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

Go back to Copper Binding Sites List in 5lm8
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

Go back to Copper Binding Sites List in 5lm8
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

Go back to Copper Binding Sites List in 5lm8
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: Wed Jul 31 04:23:40 2024

Last articles

Ca in 5UVE
Ca in 5UW5
Ca in 5UW6
Ca in 5UVL
Ca in 5UVG
Ca in 5UUE
Ca in 5UUY
Ca in 5UUH
Ca in 5UUG
Ca in 5UUD
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy