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Copper in PDB 2xyb: Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus

Enzymatic activity of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus

All present enzymatic activity of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus, PDB code: 2xyb was solved by K.Piontek, T.Choinowski, M.Antorini, I.Herpoel-Gimbert, D.A.Plattner, J.C.Sigoillot, M.Asther, K.Winterhalter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.55 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.296, 62.902, 91.416, 90.00, 126.70, 90.00
R / Rfree (%) 16.4 / 20.8

Other elements in 2xyb:

The structure of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus also contains other interesting chemical elements:

Sodium (Na) 1 atom
Zinc (Zn) 8 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus (pdb code 2xyb). 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 Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus, PDB code: 2xyb:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2xyb

Go back to Copper Binding Sites List in 2xyb
Copper binding site 1 out of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus


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 Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:29.4
occ:1.00
ND1 A:HIS456 2.0 27.0 1.0
ND1 A:HIS395 2.1 27.4 1.0
SG A:CYS451 2.3 25.3 1.0
CE1 A:HIS456 3.0 27.4 1.0
CE1 A:HIS395 3.0 33.0 1.0
CG A:HIS456 3.0 25.2 1.0
CG A:HIS395 3.1 28.6 1.0
CB A:CYS451 3.3 20.0 1.0
CB A:HIS456 3.4 27.1 1.0
CB A:HIS395 3.5 24.1 1.0
CD1 A:ILE453 3.6 24.1 1.0
CD2 A:PHE461 3.7 22.9 1.0
CB A:ILE453 3.8 22.0 1.0
CE2 A:PHE461 3.9 20.7 1.0
CA A:HIS395 3.9 26.5 1.0
CG1 A:ILE453 4.0 21.6 1.0
NE2 A:HIS456 4.1 25.7 1.0
NE2 A:HIS395 4.1 27.8 1.0
CD2 A:HIS456 4.2 28.0 1.0
CD2 A:HIS395 4.2 29.1 1.0
CG2 A:ILE453 4.6 25.9 1.0
CD A:PRO396 4.6 21.5 1.0
O A:GLY392 4.6 31.4 1.0
CA A:CYS451 4.7 19.2 1.0
N A:ILE453 4.7 25.2 1.0
CA A:ILE453 4.8 22.4 1.0
CA A:HIS456 4.9 25.2 1.0
C A:HIS395 4.9 28.3 1.0
CG A:PHE461 5.0 25.4 1.0

Copper binding site 2 out of 4 in 2xyb

Go back to Copper Binding Sites List in 2xyb
Copper binding site 2 out of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus


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 Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:29.7
occ:1.00
O2 A:PER505 1.8 27.5 1.0
NE2 A:HIS400 2.0 24.1 1.0
NE2 A:HIS111 2.1 28.8 1.0
NE2 A:HIS450 2.1 25.1 1.0
CE1 A:HIS400 2.7 25.9 1.0
O1 A:PER505 3.0 30.0 1.0
CE1 A:HIS111 3.0 24.1 1.0
CD2 A:HIS111 3.1 25.8 1.0
CD2 A:HIS450 3.1 23.8 1.0
CE1 A:HIS450 3.1 28.4 1.0
CD2 A:HIS400 3.2 25.3 1.0
CD2 A:HIS398 3.6 23.2 1.0
O A:HOH935 3.9 32.7 1.0
ND1 A:HIS400 4.0 24.2 1.0
ND1 A:HIS111 4.1 24.2 1.0
CU A:CU504 4.1 36.0 1.0
ND1 A:HIS450 4.2 21.0 1.0
CG A:HIS111 4.2 23.9 1.0
CG A:HIS400 4.2 26.3 1.0
CG A:HIS450 4.2 25.1 1.0
NE2 A:HIS398 4.3 23.4 1.0
CD2 A:PHE448 4.3 25.0 1.0
CD2 A:HIS64 4.4 22.9 1.0
NE2 A:HIS64 4.6 23.3 1.0
CB A:PHE448 4.6 26.5 1.0
CG A:PRO79 4.7 21.7 1.0
NE2 A:HIS452 4.7 25.9 1.0
CU A:CU503 4.7 25.3 1.0
CG A:HIS398 4.7 27.3 1.0
CD2 A:HIS452 4.8 22.7 1.0
CE1 A:HIS109 4.9 21.0 1.0
CG A:PHE448 5.0 26.9 1.0

Copper binding site 3 out of 4 in 2xyb

Go back to Copper Binding Sites List in 2xyb
Copper binding site 3 out of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus


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 Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:25.3
occ:1.00
O1 A:PER505 1.8 30.0 1.0
ND1 A:HIS66 2.0 22.4 1.0
NE2 A:HIS109 2.0 19.4 1.0
NE2 A:HIS452 2.1 25.9 1.0
CE1 A:HIS66 2.9 21.6 1.0
CE1 A:HIS452 2.9 25.0 1.0
CE1 A:HIS109 3.0 21.0 1.0
O2 A:PER505 3.0 27.5 1.0
CD2 A:HIS109 3.1 19.4 1.0
CG A:HIS66 3.1 22.1 1.0
CD2 A:HIS452 3.2 22.7 1.0
CB A:HIS66 3.5 19.1 1.0
CZ2 A:TRP107 3.8 18.8 1.0
CD2 A:HIS64 3.9 22.9 1.0
CU A:CU504 4.0 36.0 1.0
CE2 A:TRP107 4.1 21.0 1.0
NE2 A:HIS66 4.1 20.3 1.0
ND1 A:HIS109 4.1 18.5 1.0
ND1 A:HIS452 4.1 21.1 1.0
NE1 A:TRP107 4.2 21.7 1.0
CD2 A:HIS66 4.2 22.5 1.0
CG A:HIS109 4.2 18.5 1.0
CD2 A:HIS398 4.3 23.2 1.0
CG A:HIS452 4.3 25.5 1.0
CB A:ALA241 4.3 19.1 1.0
O A:HOH935 4.4 32.7 1.0
NE2 A:HIS64 4.4 23.3 1.0
NE2 A:HIS398 4.5 23.4 1.0
CH2 A:TRP107 4.5 21.8 1.0
CA A:HIS66 4.6 22.1 1.0
CU A:CU502 4.7 29.7 1.0
CD2 A:TRP107 5.0 19.2 1.0

Copper binding site 4 out of 4 in 2xyb

Go back to Copper Binding Sites List in 2xyb
Copper binding site 4 out of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus


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 Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:36.0
occ:1.00
NE2 A:HIS398 2.0 23.4 1.0
NE2 A:HIS64 2.0 23.3 1.0
O A:HOH874 2.8 26.6 1.0
CD2 A:HIS398 2.9 23.2 1.0
CE1 A:HIS398 2.9 25.2 1.0
CD2 A:HIS64 2.9 22.9 1.0
CE1 A:HIS64 3.0 24.5 1.0
O1 A:PER505 3.1 30.0 1.0
ND1 A:HIS66 3.4 22.4 1.0
NE2 A:HIS400 3.4 24.1 1.0
CE1 A:HIS400 3.5 25.9 1.0
CD2 A:HIS400 3.6 25.3 1.0
CG A:HIS66 3.7 22.1 1.0
CE1 A:HIS66 3.7 21.6 1.0
ND1 A:HIS400 3.8 24.2 1.0
O2 A:PER505 3.8 27.5 1.0
CA A:HIS66 3.9 22.1 1.0
CG A:HIS400 3.9 26.3 1.0
CU A:CU503 4.0 25.3 1.0
CG A:HIS398 4.0 27.3 1.0
ND1 A:HIS64 4.0 20.5 1.0
ND1 A:HIS398 4.0 27.1 1.0
CG A:HIS64 4.0 20.8 1.0
CD2 A:HIS66 4.1 22.5 1.0
CB A:HIS66 4.1 19.1 1.0
CU A:CU502 4.1 29.7 1.0
N A:GLY67 4.2 17.8 1.0
NE2 A:HIS66 4.2 20.3 1.0
C A:HIS66 4.6 17.6 1.0
O A:HOH748 4.6 27.6 1.0
CA A:HIS400 4.7 22.7 1.0
CB A:HIS400 4.8 20.1 1.0
O A:HOH993 4.8 32.3 1.0
N A:HIS66 4.9 20.6 1.0
O A:TRP65 5.0 20.3 1.0

Reference:

K.Piontek, T.Choinowski, M.Antorini, I.Herpoel-Gimbert, M.Asther, D.A.Plattner. Substrate Binding and Copper Geometry in Laccases To Be Published.
Page generated: Mon Jul 14 01:38:13 2025

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