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Copper in PDB 3kw8: Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution

Enzymatic activity of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution

All present enzymatic activity of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution:
1.10.3.2;

Protein crystallography data

The structure of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution, PDB code: 3kw8 was solved by T.Skalova, J.Dohnalek, P.Kolenko, J.Duskova, A.Stepankova, J.Hasek, L.H.Ostergaard, P.R.Ostergaard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.56 / 2.29
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 176.723, 176.723, 176.723, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 17.8

Copper Binding Sites:

The binding sites of Copper atom in the Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution (pdb code 3kw8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution, PDB code: 3kw8:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3kw8

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Copper binding site 1 out of 4 in the Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:26.5
occ:1.00
ND1 A:HIS293 1.9 23.1 1.0
ND1 A:HIS231 2.0 24.4 1.0
SG A:CYS288 2.2 25.2 1.0
CE1 A:HIS293 2.9 28.4 1.0
CE1 A:HIS231 2.9 24.0 1.0
CG A:HIS293 3.0 27.1 1.0
CG A:HIS231 3.0 22.7 1.0
CB A:CYS288 3.2 23.4 1.0
CB A:HIS293 3.3 27.4 1.0
CB A:HIS231 3.3 23.2 1.0
SD A:MET298 3.5 27.6 1.0
CA A:HIS231 3.7 23.1 1.0
NE2 A:HIS293 4.0 26.9 1.0
CG2 A:VAL290 4.0 21.0 1.0
CE A:MET298 4.0 23.6 1.0
NE2 A:HIS231 4.1 23.6 1.0
O A:TYR230 4.1 22.9 1.0
CD2 A:HIS293 4.1 27.1 1.0
CB A:VAL290 4.1 24.2 1.0
CD2 A:HIS231 4.1 21.7 1.0
CA A:CYS288 4.6 23.8 1.0
N A:THR232 4.6 22.6 1.0
N A:HIS231 4.7 23.1 1.0
C A:HIS231 4.8 22.9 1.0
C A:TYR230 4.8 23.2 1.0
CA A:HIS293 4.8 27.9 1.0
CD2 A:PHE195 5.0 25.9 1.0
CG1 A:VAL290 5.0 21.4 1.0
N A:VAL290 5.0 24.1 1.0

Copper binding site 2 out of 4 in 3kw8

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Copper binding site 2 out of 4 in the Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu402

b:29.5
occ:1.00
NE2 A:HIS289 2.1 21.2 1.0
O A:HOH701 2.7 41.5 1.0
CD2 A:HIS289 3.0 20.2 1.0
CE1 A:HIS289 3.1 23.6 1.0
CU A:CU404 3.9 48.2 0.3
CG A:HIS289 4.1 24.3 1.0
ND1 A:HIS289 4.2 24.0 1.0
NE2 A:HIS234 4.3 25.0 1.0
CD2 A:HIS234 4.4 25.1 1.0
O A:HOH929 4.7 34.5 1.0
CE1 A:HIS234 4.9 26.7 1.0
CU A:CU403 4.9 40.9 0.7

Copper binding site 3 out of 4 in 3kw8

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Copper binding site 3 out of 4 in the Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu403

b:40.9
occ:0.70
NE2 A:HIS236 2.0 24.0 1.0
O A:HOH701 2.3 41.5 1.0
NE2 A:HIS287 2.4 26.9 1.0
CE1 A:HIS236 2.8 24.8 1.0
CD2 A:HIS236 3.2 26.0 1.0
CE1 A:HIS287 3.3 26.8 1.0
CD2 A:HIS287 3.3 29.4 1.0
O A:HOH929 3.7 34.5 1.0
CU A:CU404 3.8 48.2 0.3
CD2 A:HIS234 4.0 25.1 1.0
ND1 A:HIS236 4.0 26.4 1.0
CG A:HIS236 4.2 24.9 1.0
NE2 A:HIS234 4.4 25.0 1.0
ND1 A:HIS287 4.4 27.8 1.0
CG A:HIS287 4.5 27.2 1.0
SD A:MET285 4.7 42.3 0.8
NE2 A:HIS289 4.8 21.2 1.0
CE A:MET285 4.9 43.8 1.0
CU A:CU402 4.9 29.5 1.0
CD2 A:HIS289 5.0 20.2 1.0

Copper binding site 4 out of 4 in 3kw8

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Copper binding site 4 out of 4 in the Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Two-Domain Laccase From Streptomyces Coelicolor at 2.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu404

b:48.2
occ:0.30
NE2 A:HIS234 2.0 25.0 1.0
O A:HOH930 2.6 31.6 1.0
CE1 A:HIS234 2.9 26.7 1.0
CD2 A:HIS234 3.0 25.1 1.0
O A:HOH701 3.0 41.5 1.0
CD2 A:HIS236 3.3 26.0 1.0
NE2 A:HIS236 3.3 24.0 1.0
CU A:CU403 3.8 40.9 0.7
CG A:HIS236 3.9 24.9 1.0
CU A:CU402 3.9 29.5 1.0
CE1 A:HIS236 3.9 24.8 1.0
ND1 A:HIS234 4.0 26.6 1.0
CG A:HIS234 4.1 24.0 1.0
ND1 A:HIS236 4.2 26.4 1.0
CA A:HIS236 4.6 24.6 1.0
CB A:HIS236 4.7 25.3 1.0
O A:HOH736 4.9 25.9 1.0
N A:HIS236 4.9 25.0 1.0

Reference:

T.Skalova, J.Duskova, J.Hasek, A.Stepankova, T.Koval, L.H.Ostergaard, J.Dohnalek. Structure of Laccase From Streptomyces Coelicolor After Soaking with Potassium Hexacyanoferrate and at An Improved Resolution of 2.3 A Acta Crystallogr.,Sect.F V. 67 27 2011.
ISSN: ESSN 1744-3091
PubMed: 21206017
DOI: 10.1107/S1744309110046099
Page generated: Fri Sep 4 08:07:56 2020
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