Copper in PDB 1gsk: Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis

The structure of Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis, PDB code: 1gsk was solved by F.J.Enguita, P.M.Matias, L.O.Martins, A.O.Henriques, M.A.Carrondo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.71 / 1.7
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.051, 102.051, 136.393, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 19.9

The binding sites of Copper atom in the Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis (pdb code 1gsk). 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 Cota, An Endospore Coat Protein From Bacillus Subtilis, PDB code: 1gsk:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis


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 Cota, An Endospore Coat Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1515 b:28.8 occ:1.00 ND1 A:HIS419 2.1 23.9 1.0 ND1 A:HIS497 2.1 24.2 1.0 SG A:CYS492 2.2 22.0 1.0 CE1 A:HIS419 2.8 24.1 1.0 CE1 A:HIS497 3.0 27.6 1.0 CG A:HIS497 3.1 22.4 1.0 CG A:HIS419 3.2 23.9 1.0 SD A:MET502 3.3 23.0 1.0 CB A:CYS492 3.3 18.8 1.0 CB A:HIS497 3.4 20.4 1.0 CB A:HIS419 3.7 23.1 1.0 CD1 A:ILE494 3.9 22.9 1.0 CE A:MET502 3.9 26.8 1.0 NE2 A:HIS419 4.0 24.0 1.0 CB A:ILE494 4.1 17.4 1.0 NE2 A:HIS497 4.2 25.2 1.0 CD2 A:HIS497 4.2 22.8 1.0 CD2 A:HIS419 4.2 25.1 1.0 CA A:HIS419 4.2 22.3 1.0 CG1 A:ILE494 4.3 18.8 1.0 CD1 A:LEU386 4.6 32.9 1.0 CA A:CYS492 4.7 18.9 1.0 CD A:PRO420 4.7 19.9 1.0 O A:HOH2412 4.7 34.2 1.0 CG A:MET502 4.8 22.1 1.0 N A:ILE494 4.8 18.9 1.0 CG2 A:ILE494 4.9 20.1 1.0 CA A:HIS497 4.9 20.8 1.0

Copper binding site 2 out of 4 in the Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis


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 Cota, An Endospore Coat Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1516 b:40.2 occ:0.50 CU2 A:C2O1516 0.0 40.2 0.5 ND1 A:HIS107 1.9 22.0 1.0 NE2 A:HIS153 2.1 20.8 1.0 NE2 A:HIS493 2.1 25.7 1.0 CE1 A:HIS107 2.2 22.1 1.0 O1 A:C2O1516 2.2 16.8 0.5 CE1 A:HIS153 2.8 19.0 1.0 CD2 A:HIS493 2.9 26.5 1.0 CE1 A:HIS493 3.1 23.3 1.0 CG A:HIS107 3.2 18.0 1.0 CD2 A:HIS153 3.2 20.2 1.0 NE2 A:HIS107 3.5 19.0 1.0 CB A:HIS107 3.9 16.1 1.0 CD2 A:HIS105 3.9 16.7 1.0 CD2 A:HIS107 3.9 18.2 1.0 CZ2 A:TRP151 4.0 17.9 1.0 O A:HOH2468 4.0 31.4 1.0 ND1 A:HIS153 4.0 18.3 1.0 CG A:HIS493 4.1 20.3 1.0 ND1 A:HIS493 4.1 23.8 1.0 CD2 A:HIS422 4.1 18.2 1.0 CB A:ALA297 4.2 16.9 1.0 CG A:HIS153 4.3 16.8 1.0 CU3 A:C2O1516 4.3 43.5 0.5 NE2 A:HIS105 4.4 18.5 1.0 CE2 A:TRP151 4.4 14.7 1.0 NE2 A:HIS422 4.4 19.6 1.0 NE1 A:TRP151 4.5 15.7 1.0 CU4 A:C1O1517 4.6 49.8 0.5 CH2 A:TRP151 4.7 18.6 1.0 CE1 A:HIS491 4.9 22.4 1.0 CG A:HIS422 4.9 17.8 1.0 CA A:HIS107 4.9 16.0 1.0

Copper binding site 3 out of 4 in the Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis


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 Cota, An Endospore Coat Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1516 b:43.5 occ:0.50 CU3 A:C2O1516 0.0 43.5 0.5 NE2 A:HIS491 2.0 25.7 1.0 NE2 A:HIS424 2.0 21.5 1.0 NE2 A:HIS155 2.1 26.4 1.0 O1 A:C2O1516 2.1 16.8 0.5 CE1 A:HIS424 2.7 20.2 1.0 CE1 A:HIS491 2.8 22.4 1.0 CD2 A:HIS155 2.9 25.7 1.0 CD2 A:HIS491 3.1 21.6 1.0 CE1 A:HIS155 3.2 25.5 1.0 CD2 A:HIS424 3.3 19.6 1.0 CD2 A:HIS422 3.4 18.2 1.0 O A:HOH2468 3.7 31.4 1.0 CD2 A:HIS105 3.8 16.7 1.0 NE2 A:HIS105 3.9 18.5 1.0 ND1 A:HIS424 3.9 17.1 1.0 ND1 A:HIS491 4.0 21.6 1.0 NE2 A:HIS422 4.1 19.6 1.0 CG A:HIS155 4.1 20.6 1.0 CG A:HIS491 4.1 18.7 1.0 ND1 A:HIS155 4.2 24.8 1.0 CG A:HIS424 4.2 17.3 1.0 CU2 A:C2O1516 4.3 40.2 0.5 CG2 A:VAL489 4.3 21.0 1.0 CG A:HIS105 4.5 16.9 1.0 CG A:HIS422 4.6 17.8 1.0 CE1 A:HIS105 4.6 19.5 1.0 CD2 A:HIS493 4.6 26.5 1.0 O A:HOH2157 4.7 26.7 1.0 CU4 A:C1O1517 4.7 49.8 0.5 NE2 A:HIS493 4.7 25.7 1.0 OE2 A:GLU498 4.7 24.2 1.0 CE1 A:HIS153 4.9 19.0 1.0 ND1 A:HIS105 4.9 17.8 1.0

Copper binding site 4 out of 4 in the Crystal Structure of Cota, An Endospore Coat Protein From Bacillus Subtilis


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 Cota, An Endospore Coat Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1517 b:49.8 occ:0.50 CU4 A:C1O1517 0.0 49.8 0.5 NE2 A:HIS105 1.9 18.5 1.0 NE2 A:HIS422 1.9 19.6 1.0 O3 A:C1O1517 2.1 28.0 0.5 CE1 A:HIS105 2.5 19.5 1.0 CE1 A:HIS422 2.6 18.6 1.0 CD2 A:HIS105 3.1 16.7 1.0 CA A:HIS107 3.1 16.0 1.0 CD2 A:HIS422 3.2 18.2 1.0 N A:GLY108 3.2 16.9 1.0 CG A:HIS107 3.4 18.0 1.0 ND1 A:HIS107 3.6 22.0 1.0 CD2 A:HIS107 3.6 18.2 1.0 C A:HIS107 3.7 17.8 1.0 ND1 A:HIS105 3.7 17.8 1.0 CB A:HIS107 3.7 16.1 1.0 ND1 A:HIS422 3.8 19.6 1.0 NE2 A:HIS107 4.0 19.0 1.0 CE1 A:HIS107 4.0 22.1 1.0 CG A:HIS105 4.0 16.9 1.0 CD2 A:HIS424 4.1 19.6 1.0 CG A:HIS422 4.1 17.8 1.0 NE2 A:HIS424 4.1 21.5 1.0 O A:LEU106 4.1 16.5 1.0 N A:HIS107 4.2 15.4 1.0 O A:HOH2153 4.2 17.8 1.0 CG A:HIS424 4.2 17.3 1.0 O1 A:C2O1516 4.2 16.8 0.5 CE1 A:HIS424 4.3 20.2 1.0 ND1 A:HIS424 4.3 17.1 1.0 O A:HOH2416 4.4 20.2 1.0 CA A:GLY108 4.5 17.7 1.0 C A:LEU106 4.5 16.9 1.0 CA A:HIS424 4.5 16.4 1.0 CU2 A:C2O1516 4.6 40.2 0.5 CU3 A:C2O1516 4.7 43.5 0.5 CB A:HIS424 4.8 17.6 1.0 O A:HIS107 4.9 17.6 1.0 O A:LEU423 5.0 19.0 1.0

F.J.Enguita, L.O.Martins, A.O.Henriques, M.A.Carrondo. Crystal Structure of A Bacterial Endospore Coat Component: A Laccase with Enhanced Thermostability Properties J.Biol.Chem. V. 278 19416 2003.
ISSN: ISSN 0021-9258
PubMed: 12637519
DOI: 10.1074/JBC.M301251200