Copper in PDB 8aip: Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300

The structure of Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300, PDB code: 8aip was solved by A.G.Gabdulkhakov, T.V.Tishchenko, L.Trubitsina, I.Trubitsin, A.Leontievsky, A.Lisov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.65 / 2.35
Space group	P 2 3
Cell size a, b, c (Å), α, β, γ (°)	97.962, 97.962, 97.962, 90, 90, 90
R / Rfree (%)	23.1 / 28.1

The binding sites of Copper atom in the Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300 (pdb code 8aip). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300, PDB code: 8aip:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300


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 Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu401 b:32.4 occ:1.00 ND1 A:HIS293 2.1 27.2 1.0 SG A:CYS288 2.1 22.5 1.0 ND1 A:HIS231 2.2 22.0 1.0 CG A:HIS293 3.0 20.6 1.0 CG A:HIS231 3.0 22.8 1.0 CE1 A:HIS293 3.1 24.0 1.0 CB A:CYS288 3.2 29.1 1.0 CB A:HIS231 3.2 20.9 1.0 CE1 A:HIS231 3.3 26.2 1.0 SD A:MET298 3.3 32.4 1.0 CB A:HIS293 3.3 24.9 1.0 CA A:HIS231 3.6 22.4 1.0 CE A:MET298 3.7 25.2 1.0 CG2 A:VAL290 4.1 20.7 1.0 O A:PHE230 4.1 19.4 1.0 CB A:VAL290 4.1 29.2 1.0 CD2 A:HIS293 4.2 21.0 1.0 NE2 A:HIS293 4.2 28.6 1.0 CD2 A:HIS231 4.2 19.1 1.0 NE2 A:HIS231 4.3 21.3 1.0 N A:HIS231 4.6 22.6 1.0 CA A:CYS288 4.6 28.0 1.0 N A:THR232 4.7 17.9 1.0 C A:PHE230 4.7 22.9 1.0 C A:HIS231 4.7 25.2 1.0 CG A:MET298 4.8 28.8 1.0 CA A:HIS293 4.8 28.7 1.0 N A:VAL290 5.0 25.8 1.0

Copper binding site 2 out of 3 in the Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300


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 Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:37.8 occ:1.00 NE2 A:HIS289 2.2 27.9 1.0 O2 A:OXY404 2.6 34.5 1.0 O1 A:OXY404 2.7 30.7 1.0 CE1 A:HIS289 3.0 23.9 1.0 CD2 A:HIS289 3.3 22.1 1.0 ND1 A:HIS289 4.2 28.5 1.0 CG A:HIS289 4.3 25.8 1.0 NE2 A:HIS234 4.5 24.8 1.0 CD2 A:HIS234 4.7 27.1 1.0 CU A:CU403 4.9 43.2 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300


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 Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu403 b:43.2 occ:1.00 NE2 A:HIS236 2.1 32.1 1.0 NE2 A:HIS287 2.2 30.9 1.0 O2 A:OXY404 2.4 34.5 1.0 O1 A:OXY404 2.5 30.7 1.0 CE1 A:HIS236 2.8 28.3 1.0 CD2 A:HIS287 3.1 32.4 1.0 CE1 A:HIS287 3.2 31.0 1.0 CD2 A:HIS236 3.3 28.1 1.0 CE A:MET285 3.7 35.9 1.0 ND1 A:HIS236 4.0 30.7 1.0 ND1 A:HIS287 4.2 32.5 1.0 CG A:HIS287 4.2 30.2 1.0 CG A:HIS236 4.3 27.6 1.0 CD2 A:HIS234 4.4 27.1 1.0 SD A:MET285 4.5 48.6 0.9 NE2 A:HIS234 4.8 24.8 1.0 NE2 A:HIS289 4.9 27.9 1.0 CU A:CU402 4.9 37.8 1.0

A.G.Gabdulkhakov, T.V.Tishchenko, L.Trubitsina, I.Trubitsin, A.Leontievsky, A.Lisov. Crystal Structure of Two-Domain Bacterial Laccase From the Actinobacterium Streptomyces Carpinensis Vkm Ac-1300 To Be Published.