Atomistry » Copper » PDB 2pp8-2vr6 » 2qt6
Atomistry »
  Copper »
    PDB 2pp8-2vr6 »
      2qt6 »

Copper in PDB 2qt6: Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus

Enzymatic activity of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus

All present enzymatic activity of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus, PDB code: 2qt6 was solved by M.Ferraroni, F.Briganti, A.Scozzafava, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.218, 111.613, 97.086, 90.00, 97.75, 90.00
R / Rfree (%) 15 / 18.2

Other elements in 2qt6:

The structure of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms
Calcium (Ca) 6 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus (pdb code 2qt6). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus, PDB code: 2qt6:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Copper binding site 1 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 1 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu499

b:19.2
occ:0.75
 ND1 A:HIS457 2.0 16.1 1.0
ND1 A:HIS394 2.0 16.7 1.0
SG A:CYS452 2.2 16.7 1.0
CE1 A:HIS394 2.9 19.2 1.0
CE1 A:HIS457 3.0 17.6 1.0
CG A:HIS457 3.0 16.4 1.0
CG A:HIS394 3.1 16.1 1.0
CB A:CYS452 3.3 15.4 1.0
CB A:HIS457 3.4 15.8 1.0
CB A:HIS394 3.5 15.4 1.0
CD1 A:ILE454 3.6 15.4 1.0
CD2 A:PHE462 3.7 14.4 1.0
CB A:ILE454 3.8 15.2 1.0
CE2 A:PHE462 3.8 16.6 1.0
CA A:HIS394 4.0 16.0 1.0
NE2 A:HIS394 4.1 17.3 1.0
CG1 A:ILE454 4.1 15.6 1.0
NE2 A:HIS457 4.1 18.2 1.0
CD2 A:HIS457 4.2 17.1 1.0
CD2 A:HIS394 4.2 16.8 1.0
CG2 A:ILE454 4.6 16.0 1.0
CD A:PRO395 4.7 16.1 1.0
CA A:CYS452 4.7 14.4 1.0
O A:GLY391 4.7 20.7 1.0
N A:ILE454 4.8 15.6 1.0
CA A:ILE454 4.8 15.6 1.0
O A:ILE454 4.9 15.5 1.0
CA A:HIS457 4.9 15.5 1.0
CG A:PHE462 5.0 14.3 1.0
C A:HIS394 5.0 16.1 1.0

Copper binding site 2 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 2 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:19.7
occ:0.50
 NE2 A:HIS397 1.9 17.5 1.0
NE2 A:HIS64 1.9 15.5 1.0
O A:HOH4600 2.2 48.4 1.0
O A:HOH4017 2.4 18.1 1.0
CE1 A:HIS64 2.8 16.1 1.0
CD2 A:HIS397 2.9 17.6 1.0
CE1 A:HIS397 2.9 17.8 1.0
CD2 A:HIS64 3.0 14.7 1.0
NE2 A:HIS399 3.3 16.8 1.0
CE1 A:HIS399 3.4 16.3 1.0
ND1 A:HIS66 3.5 15.6 1.0
CD2 A:HIS399 3.6 16.0 1.0
ND1 A:HIS399 3.6 14.7 1.0
CG A:HIS66 3.7 14.7 1.0
CG A:HIS399 3.7 15.0 1.0
CE1 A:HIS66 3.8 16.7 1.0
CA A:HIS66 3.9 16.4 1.0
N A:GLY67 3.9 16.0 1.0
ND1 A:HIS64 3.9 16.3 1.0
ND1 A:HIS397 4.0 17.3 1.0
CG A:HIS397 4.0 16.1 1.0
CG A:HIS64 4.0 15.9 1.0
CU A:CU502 4.1 21.2 0.8
O A:HOH3898 4.1 21.8 0.8
CD2 A:HIS66 4.1 16.1 1.0
NE2 A:HIS66 4.2 16.1 1.0
CB A:HIS66 4.2 16.0 1.0
CU A:CU501 4.3 22.4 0.8
C A:HIS66 4.4 16.3 1.0
O A:HOH4054 4.5 19.5 1.0
CA A:HIS399 4.6 15.2 1.0
CB A:HIS399 4.7 14.0 1.0
O A:HOH4012 4.7 19.9 1.0
CA A:GLY67 5.0 15.9 1.0
N A:HIS66 5.0 15.1 1.0

Copper binding site 3 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 3 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:22.4
occ:0.75
 NE2 A:HIS399 2.0 16.8 1.0
NE2 A:HIS451 2.0 16.7 1.0
NE2 A:HIS111 2.0 16.4 1.0
O A:HOH3898 2.2 21.8 0.8
CE1 A:HIS399 2.8 16.3 1.0
O A:HOH4600 2.9 48.4 1.0
CE1 A:HIS451 3.0 16.9 1.0
CE1 A:HIS111 3.0 14.8 1.0
CD2 A:HIS451 3.0 15.9 1.0
CD2 A:HIS111 3.1 16.7 1.0
CD2 A:HIS399 3.1 16.0 1.0
CD2 A:HIS397 3.8 17.6 1.0
O A:HOH4152 3.8 24.5 1.0
ND1 A:HIS399 4.0 14.7 1.0
ND1 A:HIS451 4.1 16.6 1.0
CG A:HIS451 4.1 15.2 1.0
ND1 A:HIS111 4.1 15.6 1.0
CG A:HIS399 4.2 15.0 1.0
CD2 A:PHE449 4.2 15.3 1.0
CG A:HIS111 4.2 15.4 1.0
CU A:CU500 4.3 19.7 0.5
CD2 A:HIS64 4.5 14.7 1.0
NE2 A:HIS397 4.5 17.5 1.0
CB A:PHE449 4.5 14.4 1.0
CG A:PRO79 4.6 15.5 1.0
NE2 A:HIS64 4.6 15.5 1.0
CG A:PHE449 4.8 14.8 1.0
NE2 A:HIS453 4.9 16.4 1.0
CD2 A:HIS453 4.9 14.8 1.0
CG A:HIS397 4.9 16.1 1.0
CU A:CU502 4.9 21.2 0.8
CE1 A:HIS109 4.9 16.2 1.0

Copper binding site 4 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 4 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:21.2
occ:0.75
 ND1 A:HIS66 2.0 15.6 1.0
NE2 A:HIS109 2.0 16.3 1.0
NE2 A:HIS453 2.1 16.4 1.0
O A:HOH4600 2.6 48.4 1.0
CE1 A:HIS66 2.9 16.7 1.0
O A:HOH3898 3.0 21.8 0.8
CD2 A:HIS109 3.0 14.5 1.0
CE1 A:HIS109 3.0 16.2 1.0
CE1 A:HIS453 3.0 16.0 1.0
CG A:HIS66 3.1 14.7 1.0
CD2 A:HIS453 3.2 14.8 1.0
CB A:HIS66 3.5 16.0 1.0
CZ2 A:TRP107 3.6 15.6 1.0
CD2 A:HIS64 3.8 14.7 1.0
CE2 A:TRP107 3.9 14.5 1.0
NE1 A:TRP107 4.0 15.4 1.0
NE2 A:HIS66 4.1 16.1 1.0
ND1 A:HIS109 4.1 16.4 1.0
CU A:CU500 4.1 19.7 0.5
CG A:HIS109 4.1 13.6 1.0
CD2 A:HIS66 4.2 16.1 1.0
ND1 A:HIS453 4.2 15.0 1.0
CG A:HIS453 4.3 14.2 1.0
NE2 A:HIS64 4.3 15.5 1.0
CB A:ALA241 4.3 15.0 1.0
CD2 A:HIS397 4.4 17.6 1.0
CH2 A:TRP107 4.4 16.0 1.0
O A:HOH4152 4.4 24.5 1.0
NE2 A:HIS397 4.5 17.5 1.0
CA A:HIS66 4.6 16.4 1.0
CD2 A:TRP107 4.8 13.7 1.0
CU A:CU501 4.9 22.4 0.8
CD1 A:TRP107 5.0 15.2 1.0

Copper binding site 5 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 5 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu499

b:24.2
occ:0.75
 ND1 B:HIS457 2.0 20.3 1.0
ND1 B:HIS394 2.0 22.0 1.0
SG B:CYS452 2.3 20.6 1.0
CE1 B:HIS394 2.9 24.1 1.0
CE1 B:HIS457 3.0 23.8 1.0
CG B:HIS457 3.0 21.2 1.0
CG B:HIS394 3.1 21.9 1.0
CB B:CYS452 3.3 18.8 1.0
CB B:HIS457 3.4 21.6 1.0
CB B:HIS394 3.5 21.2 1.0
CD1 B:ILE454 3.6 20.2 1.0
CD2 B:PHE462 3.7 20.7 1.0
CB B:ILE454 3.8 18.5 1.0
CE2 B:PHE462 3.8 21.7 1.0
CA B:HIS394 4.0 21.0 1.0
NE2 B:HIS394 4.1 24.4 1.0
CG1 B:ILE454 4.1 18.6 1.0
NE2 B:HIS457 4.1 22.3 1.0
CD2 B:HIS457 4.1 22.6 1.0
CD2 B:HIS394 4.2 24.3 1.0
CG2 B:ILE454 4.6 18.6 1.0
CD B:PRO395 4.6 19.4 1.0
CA B:CYS452 4.7 18.6 1.0
O B:GLY391 4.7 27.0 1.0
N B:ILE454 4.8 18.3 1.0
CA B:HIS457 4.9 20.9 1.0
CA B:ILE454 4.9 19.1 1.0
O B:ILE454 4.9 20.2 1.0
C B:HIS394 5.0 19.7 1.0
CG B:PHE462 5.0 21.1 1.0

Copper binding site 6 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 6 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu500

b:23.9
occ:0.50
 NE2 B:HIS64 1.9 18.5 1.0
NE2 B:HIS397 1.9 20.0 1.0
O B:HOH3988 2.5 20.9 1.0
CE1 B:HIS64 2.8 19.4 1.0
CE1 B:HIS397 2.9 21.3 1.0
CD2 B:HIS397 2.9 19.1 1.0
CD2 B:HIS64 2.9 18.6 1.0
O1 B:PER503 3.1 33.7 0.8
NE2 B:HIS399 3.4 17.9 1.0
ND1 B:HIS66 3.5 18.5 1.0
CE1 B:HIS399 3.5 18.4 1.0
CD2 B:HIS399 3.6 18.2 1.0
ND1 B:HIS399 3.7 17.3 1.0
CG B:HIS66 3.7 17.5 1.0
CG B:HIS399 3.8 18.0 1.0
CE1 B:HIS66 3.8 17.8 1.0
ND1 B:HIS64 3.9 18.9 1.0
CA B:HIS66 3.9 17.6 1.0
N B:GLY67 3.9 17.6 1.0
ND1 B:HIS397 4.0 19.1 1.0
CG B:HIS397 4.0 19.7 1.0
CG B:HIS64 4.0 18.4 1.0
CU B:CU502 4.1 24.1 0.8
CD2 B:HIS66 4.2 17.3 1.0
O2 B:PER503 4.2 23.6 0.8
NE2 B:HIS66 4.2 16.9 1.0
CB B:HIS66 4.2 17.6 1.0
CU B:CU501 4.3 26.9 0.8
C B:HIS66 4.5 17.6 1.0
O B:HOH4002 4.5 21.2 1.0
CA B:HIS399 4.5 16.5 1.0
O B:HOH4009 4.6 20.8 1.0
CB B:HIS399 4.6 17.4 1.0
CA B:GLY67 5.0 17.7 1.0

Copper binding site 7 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 7 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:26.9
occ:0.75
 NE2 B:HIS111 2.0 19.9 1.0
NE2 B:HIS399 2.0 17.9 1.0
NE2 B:HIS451 2.0 22.1 1.0
O2 B:PER503 2.1 23.6 0.8
CE1 B:HIS399 2.9 18.4 1.0
O1 B:PER503 3.0 33.7 0.8
CE1 B:HIS111 3.0 19.7 1.0
CD2 B:HIS111 3.0 17.1 1.0
CE1 B:HIS451 3.0 18.5 1.0
CD2 B:HIS451 3.0 18.4 1.0
CD2 B:HIS399 3.1 18.2 1.0
O B:HOH4069 3.8 27.4 1.0
CD2 B:HIS397 3.8 19.1 1.0
ND1 B:HIS399 4.0 17.3 1.0
ND1 B:HIS111 4.1 18.7 1.0
ND1 B:HIS451 4.1 19.0 1.0
CG B:HIS111 4.1 17.8 1.0
CG B:HIS451 4.1 18.3 1.0
CG B:HIS399 4.2 18.0 1.0
CD2 B:PHE449 4.3 20.6 1.0
CU B:CU500 4.3 23.9 0.5
CD2 B:HIS64 4.4 18.6 1.0
NE2 B:HIS397 4.5 20.0 1.0
CG B:PRO79 4.6 19.5 1.0
CB B:PHE449 4.6 18.9 1.0
NE2 B:HIS64 4.6 18.5 1.0
NE2 B:HIS453 4.9 16.7 1.0
CG B:PHE449 4.9 18.8 1.0
CD2 B:HIS453 4.9 17.9 1.0
CU B:CU502 4.9 24.1 0.8
CG B:HIS397 4.9 19.7 1.0
CE1 B:HIS109 4.9 17.8 1.0

Copper binding site 8 out of 8 in 2qt6

Go back to Copper Binding Sites List in 2qt6
Copper binding site 8 out of 8 in the Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure Determination of A Blue Laccase From Lentinus Tigrinus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:24.1
occ:0.75
 ND1 B:HIS66 2.0 18.5 1.0
NE2 B:HIS109 2.0 18.3 1.0
O1 B:PER503 2.0 33.7 0.8
NE2 B:HIS453 2.1 16.7 1.0
CE1 B:HIS66 2.9 17.8 1.0
CE1 B:HIS109 3.0 17.8 1.0
CE1 B:HIS453 3.0 17.0 1.0
CD2 B:HIS109 3.0 16.6 1.0
O2 B:PER503 3.0 23.6 0.8
CG B:HIS66 3.1 17.5 1.0
CD2 B:HIS453 3.2 17.9 1.0
CB B:HIS66 3.5 17.6 1.0
CZ2 B:TRP107 3.6 16.9 1.0
CD2 B:HIS64 3.8 18.6 1.0
CE2 B:TRP107 3.9 16.2 1.0
NE1 B:TRP107 4.0 16.8 1.0
NE2 B:HIS66 4.0 16.9 1.0
ND1 B:HIS109 4.1 17.8 1.0
CU B:CU500 4.1 23.9 0.5
CG B:HIS109 4.1 16.7 1.0
CD2 B:HIS66 4.1 17.3 1.0
ND1 B:HIS453 4.1 16.8 1.0
CG B:HIS453 4.3 16.3 1.0
NE2 B:HIS64 4.3 18.5 1.0
CB B:ALA241 4.3 15.7 1.0
O B:HOH4069 4.4 27.4 1.0
CD2 B:HIS397 4.4 19.1 1.0
CH2 B:TRP107 4.4 16.3 1.0
NE2 B:HIS397 4.5 20.0 1.0
CA B:HIS66 4.6 17.6 1.0
CD2 B:TRP107 4.9 14.7 1.0
CU B:CU501 4.9 26.9 0.8
CD1 B:TRP107 5.0 16.0 1.0
CG B:HIS64 5.0 18.4 1.0

Reference:

M.Ferraroni, N.M.Myasoedova, V.Schmatchenko, A.A.Leontievsky, L.A.Golovleva, A.Scozzafava, F.Briganti. Crystal Structure of A Blue Laccase From Lentinus Tigrinus: Evidences For Intermediates in the Molecular Oxygen Reductive Splitting By Multicopper Oxidases. Bmc Struct.Biol. V. 7 60 2007.
ISSN: ESSN 1472-6807
PubMed: 17897461
DOI: 10.1186/1472-6807-7-60
Page generated: Wed Jul 31 00:00:40 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy