Copper in PDB 5l2v: Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes

The structure of Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes, PDB code: 5l2v was solved by S.H.Light, M.Agostoni, M.A.Marletta, W.F.Anderson, Center For Structuralgenomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.15 / 1.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	61.575, 139.712, 90.591, 90.00, 90.00, 90.00
R / Rfree (%)	12.9 / 14.5

The binding sites of Copper atom in the Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes (pdb code 5l2v). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes, PDB code: 5l2v:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:10.6 occ:0.75 HD1 A:HIS1 1.2 12.4 1.0 HE2 A:HIS85 1.2 12.1 1.0 H1 A:HIS1 1.8 9.6 1.0 H2 A:HIS1 1.9 9.1 1.0 ND1 A:HIS1 2.0 12.8 1.0 NE2 A:HIS85 2.0 12.7 1.0 N A:HIS1 2.2 9.2 1.0 H3 A:HIS1 2.9 8.9 1.0 CG A:HIS1 2.9 11.1 1.0 CE1 A:HIS85 3.0 13.4 1.0 CE1 A:HIS1 3.0 14.4 1.0 CD2 A:HIS85 3.0 11.7 1.0 HZ A:PHE156 3.0 8.4 1.0 O A:HOH706 3.1 33.5 1.0 CA A:HIS1 3.1 8.2 1.0 HE1 A:HIS85 3.2 13.7 1.0 HD2 A:HIS85 3.2 11.6 1.0 HB3 A:ALA83 3.2 10.2 1.0 HE1 A:HIS1 3.2 14.7 1.0 HB2 A:HIS1 3.2 9.6 1.0 CB A:HIS1 3.3 9.4 1.0 HA A:HIS1 3.4 8.1 1.0 CZ A:PHE156 3.7 8.3 1.0 HB2 A:ALA83 3.9 10.3 1.0 O A:ALA83 3.9 9.7 1.0 CB A:ALA83 4.0 10.4 1.0 O A:HOH698 4.1 26.7 1.0 CD2 A:HIS1 4.1 12.3 1.0 NE2 A:HIS1 4.1 14.5 1.0 HE1 A:PHE156 4.1 7.9 1.0 ND1 A:HIS85 4.1 13.2 1.0 CG A:HIS85 4.1 11.6 1.0 CE1 A:PHE156 4.2 8.1 1.0 HB3 A:HIS1 4.2 9.3 1.0 O A:HOH707 4.2 28.8 1.0 C A:HIS1 4.5 7.2 1.0 CE2 A:PHE156 4.5 8.2 1.0 HE2 A:PHE156 4.5 8.3 1.0 HB1 A:ALA83 4.6 10.2 1.0 O A:HOH664 4.8 36.6 1.0 O A:HIS1 4.9 7.5 1.0 C A:ALA83 4.9 9.2 1.0 HE2 A:HIS1 4.9 14.2 1.0 HZ3 A:TRP147 4.9 7.9 1.0 HD1 A:HIS85 4.9 13.1 1.0 HH2 A:TRP147 4.9 8.1 1.0 HD2 A:HIS1 4.9 12.3 1.0 CA A:ALA83 5.0 9.3 1.0

Copper binding site 2 out of 2 in the Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:18.2 occ:0.75 HD1 B:HIS1 1.2 18.8 1.0 HE2 B:HIS85 1.3 21.0 1.0 H1 B:HIS1 1.8 16.3 1.0 H2 B:HIS1 1.9 15.3 1.0 ND1 B:HIS1 2.0 19.1 1.0 NE2 B:HIS85 2.1 22.1 1.0 N B:HIS1 2.2 15.4 1.0 H3 B:HIS1 3.0 15.2 1.0 CG B:HIS1 3.0 17.2 1.0 HZ B:PHE156 3.0 13.2 1.0 CE1 B:HIS1 3.0 20.6 1.0 O B:HOH517 3.0 42.8 1.0 CD2 B:HIS85 3.1 20.2 1.0 CE1 B:HIS85 3.1 22.6 1.0 CA B:HIS1 3.2 14.3 1.0 HD2 B:HIS85 3.2 19.7 1.0 HE1 B:HIS1 3.2 20.3 1.0 HB2 B:HIS1 3.3 16.3 1.0 HB3 B:ALA83 3.3 17.2 1.0 CB B:HIS1 3.3 15.8 1.0 HE1 B:HIS85 3.3 23.8 1.0 HA B:HIS1 3.4 13.8 1.0 CZ B:PHE156 3.7 13.1 1.0 HB2 B:ALA83 3.9 17.8 1.0 O B:ALA83 3.9 17.8 1.0 CB B:ALA83 4.0 17.7 1.0 O B:HOH494 4.1 35.7 1.0 HE1 B:PHE156 4.1 12.6 1.0 NE2 B:HIS1 4.1 19.8 1.0 CD2 B:HIS1 4.1 18.1 1.0 O B:HOH518 4.2 34.9 1.0 ND1 B:HIS85 4.2 23.0 1.0 CG B:HIS85 4.2 20.5 1.0 CE1 B:PHE156 4.2 12.7 1.0 HB3 B:HIS1 4.3 15.7 1.0 CE2 B:PHE156 4.5 12.7 1.0 C B:HIS1 4.5 12.8 1.0 HE2 B:PHE156 4.5 12.9 1.0 HB1 B:ALA83 4.6 18.0 1.0 C B:ALA83 4.8 17.4 1.0 O B:HIS1 4.9 13.3 1.0 HE2 B:HIS1 4.9 19.0 1.0 HZ3 B:TRP147 4.9 12.5 1.0 H B:ALA83 5.0 16.1 1.0 CA B:ALA83 5.0 17.7 1.0 HD2 B:HIS1 5.0 18.0 1.0 HH2 B:TRP147 5.0 12.8 1.0 HD1 B:HIS85 5.0 23.0 1.0

S.H.Light, M.Agostoni, M.A.Marletta, W.F.Anderson. Catalytic Domain of Lpmo LMO2467 From Listeria Monocytogenes To Be Published.