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Copper in PDB 3tas: Small Laccase From Streptomyces Viridosporus T7A

Enzymatic activity of Small Laccase From Streptomyces Viridosporus T7A

All present enzymatic activity of Small Laccase From Streptomyces Viridosporus T7A:
1.10.3.2;

Protein crystallography data

The structure of Small Laccase From Streptomyces Viridosporus T7A, PDB code: 3tas was solved by T.Lukk, S.Majumdar, J.A.Gerlt, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.69 / 2.30
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 102.300, 157.180, 162.330, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 19.3

Other elements in 3tas:

The structure of Small Laccase From Streptomyces Viridosporus T7A also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Copper Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Copper atom in the Small Laccase From Streptomyces Viridosporus T7A (pdb code 3tas). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 15 binding sites of Copper where determined in the Small Laccase From Streptomyces Viridosporus T7A, PDB code: 3tas:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 15 in 3tas

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Copper binding site 1 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu5

b:16.2
occ:1.00
ND1 A:HIS226 2.0 12.8 1.0
ND1 A:HIS288 2.1 9.4 1.0
SG A:CYS283 2.2 17.0 1.0
CE1 A:HIS226 3.0 16.8 1.0
CG A:HIS288 3.0 11.9 1.0
CG A:HIS226 3.0 15.0 1.0
CE1 A:HIS288 3.1 11.4 1.0
CB A:CYS283 3.2 13.1 1.0
CB A:HIS288 3.2 7.4 1.0
CB A:HIS226 3.4 11.9 1.0
SD A:MET293 3.5 16.5 1.0
CE A:MET293 3.7 78.3 1.0
CA A:HIS226 3.8 16.3 1.0
O A:HOH488 4.1 39.3 1.0
NE2 A:HIS226 4.1 15.6 1.0
O A:TYR225 4.1 20.1 1.0
CG2 A:VAL285 4.1 3.4 1.0
CD2 A:HIS288 4.1 13.3 1.0
CB A:VAL285 4.1 13.1 1.0
CD2 A:HIS226 4.1 13.4 1.0
NE2 A:HIS288 4.2 11.4 1.0
CA A:CYS283 4.6 11.4 1.0
CA A:HIS288 4.7 11.2 1.0
N A:THR227 4.8 14.0 1.0
N A:HIS226 4.8 17.6 1.0
C A:TYR225 4.9 19.4 1.0
C A:HIS226 4.9 16.6 1.0
CG A:MET293 4.9 21.8 1.0
CD2 A:PHE190 4.9 12.8 1.0

Copper binding site 2 out of 15 in 3tas

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Copper binding site 2 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu7

b:15.7
occ:1.00
NE2 B:HIS97 2.0 17.1 1.0
O2 A:OXY344 2.0 4.8 1.0
NE2 A:HIS229 2.0 13.6 1.0
CE1 B:HIS97 2.9 15.5 1.0
CE1 A:HIS229 3.0 11.9 1.0
CD2 B:HIS97 3.1 14.9 1.0
CD2 A:HIS229 3.1 12.9 1.0
O1 A:OXY344 3.1 2.7 1.0
O B:HOH413 3.1 23.4 1.0
CD2 A:HIS231 3.4 11.0 1.0
NE2 A:HIS231 3.5 9.7 1.0
NE2 B:HIS99 3.5 13.7 1.0
CD2 B:HIS99 3.7 13.8 1.0
CU B:CU6 3.8 15.6 1.0
CG A:HIS231 3.9 11.3 1.0
CE1 A:HIS231 3.9 15.8 1.0
CE1 B:HIS99 4.0 12.9 1.0
ND1 B:HIS97 4.0 14.8 1.0
ND1 A:HIS229 4.1 17.3 1.0
ND1 A:HIS231 4.1 12.0 1.0
CG B:HIS97 4.1 18.1 1.0
CG A:HIS229 4.2 16.1 1.0
CU A:CU8 4.2 14.7 1.0
CG B:HIS99 4.3 17.6 1.0
O B:VAL98 4.3 9.5 1.0
ND1 B:HIS99 4.4 18.3 1.0
CA A:HIS231 4.4 9.5 1.0
CB A:HIS231 4.7 7.8 1.0
OH B:TYR103 4.9 18.2 1.0
C B:VAL98 4.9 11.3 1.0
N A:HIS231 4.9 13.6 1.0
OD2 A:ASP254 4.9 18.1 1.0
CA B:HIS99 5.0 9.5 1.0

Copper binding site 3 out of 15 in 3tas

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Copper binding site 3 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu8

b:14.7
occ:1.00
NE2 A:HIS231 2.1 9.7 1.0
NE2 B:HIS153 2.2 18.4 1.0
NE2 A:HIS282 2.3 13.2 1.0
O A:ACT347 2.4 45.5 1.0
O1 A:OXY344 2.5 2.7 1.0
O2 A:OXY344 2.8 4.8 1.0
CE1 A:HIS231 2.9 15.8 1.0
OXT A:ACT347 2.9 34.6 1.0
CE1 B:HIS153 3.0 17.0 1.0
C A:ACT347 3.1 39.0 1.0
CE1 A:HIS282 3.1 14.3 1.0
CD2 B:HIS153 3.2 20.0 1.0
CD2 A:HIS231 3.2 11.0 1.0
CD2 A:HIS282 3.3 14.3 1.0
ND1 A:HIS231 4.1 12.0 1.0
ND1 B:HIS153 4.2 15.3 1.0
ND1 A:HIS282 4.2 19.3 1.0
CU A:CU7 4.2 15.7 1.0
CG A:HIS231 4.3 11.3 1.0
CG B:HIS153 4.3 15.3 1.0
CD2 A:HIS229 4.3 12.9 1.0
CG A:HIS282 4.4 16.5 1.0
CH3 A:ACT347 4.5 30.7 1.0
NE2 B:HIS97 4.6 17.1 1.0
CE A:MET280 4.6 33.4 1.0
NE2 A:HIS229 4.7 13.6 1.0
CD2 B:HIS97 4.9 14.9 1.0
SD A:MET280 4.9 34.2 1.0
NE2 A:HIS284 4.9 12.4 1.0
CU B:CU6 4.9 15.6 1.0
ND1 B:HIS159 5.0 24.1 1.0

Copper binding site 4 out of 15 in 3tas

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Copper binding site 4 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu11

b:16.3
occ:1.00
NE2 C:HIS229 2.0 17.7 1.0
NE2 A:HIS97 2.1 13.1 1.0
O2 C:OXY3 2.1 8.0 1.0
CE1 C:HIS229 2.9 16.6 1.0
CE1 A:HIS97 3.0 17.9 1.0
CD2 C:HIS229 3.0 16.4 1.0
CD2 A:HIS97 3.1 17.3 1.0
O1 C:OXY3 3.1 9.3 1.0
NE2 C:HIS231 3.4 16.0 1.0
NE2 A:HIS99 3.5 14.7 1.0
O A:HOH403 3.5 21.2 1.0
CD2 C:HIS231 3.5 18.5 1.0
CD2 A:HIS99 3.6 20.3 1.0
CU A:CU12 3.7 17.0 1.0
CE1 C:HIS231 3.8 15.7 1.0
CG C:HIS231 3.9 17.0 1.0
ND1 C:HIS229 4.0 20.7 1.0
CE1 A:HIS99 4.0 15.3 1.0
ND1 C:HIS231 4.1 17.0 1.0
CG C:HIS229 4.1 17.3 1.0
ND1 A:HIS97 4.1 17.3 1.0
CG A:HIS97 4.2 16.1 1.0
CU C:CU10 4.2 18.5 1.0
CG A:HIS99 4.3 18.1 1.0
O A:VAL98 4.5 11.3 1.0
ND1 A:HIS99 4.5 12.2 1.0
CA C:HIS231 4.5 13.2 1.0
CB C:HIS231 4.8 15.4 1.0
N C:HIS231 4.9 14.0 1.0
C A:VAL98 5.0 11.3 1.0
O C:HOH437 5.0 15.6 1.0

Copper binding site 5 out of 15 in 3tas

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Copper binding site 5 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu12

b:17.0
occ:1.00
NE2 A:HIS99 2.1 14.7 1.0
NE2 A:HIS151 2.2 9.6 1.0
NE2 C:HIS284 2.2 18.3 1.0
O1 C:OXY3 2.5 9.3 1.0
O2 C:OXY3 2.7 8.0 1.0
CD2 A:HIS99 3.0 20.3 1.0
CE1 A:HIS151 3.1 9.8 1.0
CD2 C:HIS284 3.1 19.0 1.0
CE1 A:HIS99 3.2 15.3 1.0
CD2 A:HIS151 3.2 10.2 1.0
CE1 C:HIS284 3.3 14.7 1.0
CU A:CU11 3.7 16.3 1.0
CD2 A:HIS97 4.1 17.3 1.0
CE1 A:HIS149 4.2 12.6 1.0
CB A:ALA261 4.2 6.5 1.0
ND1 A:HIS151 4.2 11.5 1.0
CG A:HIS99 4.2 18.1 1.0
ND1 A:HIS99 4.2 12.2 1.0
OXT C:ACT347 4.3 36.5 1.0
NE2 C:HIS229 4.3 17.7 1.0
CG C:HIS284 4.3 16.8 1.0
CG A:HIS151 4.3 8.4 1.0
ND1 C:HIS284 4.3 17.8 1.0
NE2 A:HIS97 4.4 13.1 1.0
CD2 C:HIS229 4.4 16.4 1.0
CE1 C:HIS229 4.9 16.6 1.0
NE2 A:HIS149 4.9 19.7 1.0
CU C:CU10 5.0 18.5 1.0

Copper binding site 6 out of 15 in 3tas

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Copper binding site 6 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu13

b:30.9
occ:1.00
NE2 A:HIS314 2.1 23.9 1.0
OXT A:ACT348 2.3 34.7 1.0
O A:ACT348 2.9 42.8 1.0
CD2 A:HIS314 3.0 24.7 1.0
C A:ACT348 3.0 39.3 1.0
CE1 A:HIS314 3.1 22.5 1.0
CG A:HIS314 4.2 25.5 1.0
ND1 A:HIS314 4.2 21.7 1.0
CB A:ALA319 4.2 12.5 1.0
CH3 A:ACT348 4.5 41.0 1.0
N A:ALA319 4.8 22.5 1.0

Copper binding site 7 out of 15 in 3tas

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Copper binding site 7 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu2

b:18.6
occ:1.00
NE2 B:HIS229 2.1 15.4 1.0
O2 C:OXY345 2.1 5.8 1.0
NE2 C:HIS97 2.1 21.6 1.0
CD2 B:HIS229 3.0 10.3 1.0
CE1 B:HIS229 3.0 14.3 1.0
CD2 C:HIS97 3.1 18.9 1.0
CE1 C:HIS97 3.1 19.9 1.0
O1 C:OXY345 3.1 10.9 1.0
O C:HOH398 3.3 29.9 1.0
NE2 C:HIS99 3.5 9.4 1.0
CD2 B:HIS231 3.5 20.6 1.0
NE2 B:HIS231 3.6 17.7 1.0
CU C:CU1 3.7 16.9 1.0
CD2 C:HIS99 3.8 9.4 1.0
CG B:HIS231 3.9 22.8 1.0
CE1 C:HIS99 3.9 9.0 1.0
CE1 B:HIS231 3.9 14.1 1.0
ND1 B:HIS231 4.1 18.8 1.0
ND1 B:HIS229 4.1 14.9 1.0
CG B:HIS229 4.2 15.0 1.0
ND1 C:HIS97 4.2 21.9 1.0
CG C:HIS97 4.2 19.6 1.0
CU B:CU3 4.2 18.2 1.0
CG C:HIS99 4.3 15.3 1.0
ND1 C:HIS99 4.3 13.9 1.0
O C:VAL98 4.4 17.0 1.0
CA B:HIS231 4.5 15.0 1.0
CB B:HIS231 4.7 18.1 1.0
OH C:TYR103 4.9 31.4 1.0
N B:HIS231 4.9 15.8 1.0
C C:VAL98 4.9 14.8 1.0
O B:HOH390 5.0 21.2 1.0
CA C:HIS99 5.0 15.3 1.0

Copper binding site 8 out of 15 in 3tas

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Copper binding site 8 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu3

b:18.2
occ:1.00
NE2 C:HIS153 2.1 14.5 1.0
NE2 B:HIS231 2.2 17.7 1.0
NE2 B:HIS282 2.2 12.7 1.0
O1 C:OXY345 2.5 10.9 1.0
O2 C:OXY345 2.6 5.8 1.0
OXT B:ACT348 2.8 34.3 1.0
O B:ACT348 2.8 33.2 1.0
CE1 B:HIS282 2.9 9.0 1.0
CE1 B:HIS231 2.9 14.1 1.0
CD2 C:HIS153 3.1 11.4 1.0
CE1 C:HIS153 3.1 13.7 1.0
C B:ACT348 3.1 33.4 1.0
CD2 B:HIS282 3.3 9.7 1.0
CD2 B:HIS231 3.3 20.6 1.0
ND1 B:HIS282 4.1 14.0 1.0
ND1 B:HIS231 4.1 18.8 1.0
CU B:CU2 4.2 18.6 1.0
CG C:HIS153 4.2 15.1 1.0
ND1 C:HIS153 4.2 16.8 1.0
CG B:HIS282 4.3 16.1 1.0
CG B:HIS231 4.3 22.8 1.0
CD2 B:HIS229 4.4 10.3 1.0
CE B:MET280 4.4 24.0 1.0
CH3 B:ACT348 4.5 22.1 1.0
NE2 C:HIS97 4.7 21.6 1.0
NE2 B:HIS229 4.8 15.4 1.0
NE2 B:HIS284 4.9 15.8 1.0
CU C:CU1 4.9 16.9 1.0
ND1 C:HIS159 4.9 26.8 1.0

Copper binding site 9 out of 15 in 3tas

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Copper binding site 9 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu4

b:16.7
occ:1.00
ND1 B:HIS288 2.0 12.2 1.0
ND1 B:HIS226 2.1 8.8 1.0
SG B:CYS283 2.3 17.0 1.0
CG B:HIS226 3.0 11.5 1.0
CG B:HIS288 3.0 13.0 1.0
CE1 B:HIS288 3.1 11.0 1.0
CB B:CYS283 3.1 13.2 1.0
CE1 B:HIS226 3.1 9.7 1.0
CB B:HIS226 3.2 11.9 1.0
CB B:HIS288 3.3 8.8 1.0
SD B:MET293 3.6 21.6 1.0
CE B:MET293 3.6 66.3 1.0
CA B:HIS226 3.8 11.3 1.0
CG2 B:VAL285 4.1 12.2 1.0
NE2 B:HIS288 4.2 13.3 1.0
CD2 B:HIS288 4.2 15.1 1.0
CD2 B:HIS226 4.2 15.1 1.0
O B:TYR225 4.2 15.3 1.0
NE2 B:HIS226 4.2 17.2 1.0
CB B:VAL285 4.3 14.8 1.0
CA B:CYS283 4.5 15.4 1.0
N B:THR227 4.6 8.9 1.0
N B:HIS226 4.8 13.0 1.0
C B:HIS226 4.8 14.6 1.0
CA B:HIS288 4.8 11.1 1.0
CD2 B:PHE190 4.9 11.9 1.0
C B:TYR225 4.9 14.9 1.0
CG B:MET293 5.0 14.4 1.0

Copper binding site 10 out of 15 in 3tas

Go back to Copper Binding Sites List in 3tas
Copper binding site 10 out of 15 in the Small Laccase From Streptomyces Viridosporus T7A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Small Laccase From Streptomyces Viridosporus T7A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu6

b:15.6
occ:1.00
NE2 B:HIS99 2.1 13.7 1.0
NE2 B:HIS151 2.1 11.5 1.0
NE2 A:HIS284 2.2 12.4 1.0
O1 A:OXY344 2.5 2.7 1.0
O2 A:OXY344 2.7 4.8 1.0
CD2 A:HIS284 3.0 11.3 1.0
CD2 B:HIS99 3.1 13.8 1.0
CE1 B:HIS151 3.1 14.4 1.0
CD2 B:HIS151 3.1 10.4 1.0
CE1 B:HIS99 3.1 12.9 1.0
CE1 A:HIS284 3.2 13.7 1.0
CU A:CU7 3.8 15.7 1.0
CD2 B:HIS97 4.0 14.9 1.0
CB B:ALA261 4.1 4.2 1.0
CE1 B:HIS149 4.1 16.1 1.0
ND1 B:HIS151 4.2 13.0 1.0
CG A:HIS284 4.2 12.1 1.0
O A:ACT347 4.2 45.5 1.0
CG B:HIS99 4.2 17.6 1.0
ND1 B:HIS99 4.2 18.3 1.0
NE2 A:HIS229 4.3 13.6 1.0
CG B:HIS151 4.3 11.5 1.0
ND1 A:HIS284 4.3 15.2 1.0
NE2 B:HIS97 4.3 17.1 1.0
CD2 A:HIS229 4.4 12.9 1.0
CE1 A:HIS229 4.9 11.9 1.0
NE2 B:HIS149 4.9 15.3 1.0
ND1 B:HIS149 4.9 15.3 1.0
CU A:CU8 4.9 14.7 1.0

Reference:

S.Majumdar, T.Lukk, J.O.Solbiati, S.Bauer, S.K.Nair, J.E.Cronan, J.A.Gerlt. Roles of Small Laccases From Streptomyces in Lignin Degradation. Biochemistry V. 53 4047 2014.
ISSN: ISSN 0006-2960
PubMed: 24870309
DOI: 10.1021/BI500285T
Page generated: Sun Dec 13 11:12:24 2020

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