Copper in PDB 2jkw: Pseudoazurin M16F

The structure of Pseudoazurin M16F, PDB code: 2jkw was solved by S.Yanagisawa, P.B.Crowley, S.J.Firbank, A.T.Lawler, D.M.Hunter, W.Mcfarlane, C.Li, T.Kohzuma, M.J.Banfield, C.Dennison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.27 / 1.6
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.930, 90.540, 35.220, 90.00, 98.55, 90.00
R / Rfree (%)	13.1 / 18

The binding sites of Copper atom in the Pseudoazurin M16F (pdb code 2jkw). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Pseudoazurin M16F, PDB code: 2jkw:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Pseudoazurin M16F


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Pseudoazurin M16F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu125 b:13.7 occ:1.00 ND1 A:HIS81 2.0 11.8 1.0 ND1 A:HIS40 2.1 11.7 1.0 SG A:CYS78 2.2 11.8 1.0 SD A:MET86 2.6 11.3 1.0 CE1 A:HIS40 3.0 12.5 1.0 CE1 A:HIS81 3.0 14.0 1.0 CG A:HIS81 3.1 12.2 1.0 CG A:HIS40 3.2 10.8 1.0 CB A:CYS78 3.2 10.0 1.0 CB A:HIS81 3.4 11.7 1.0 CE A:MET86 3.5 11.9 1.0 CB A:HIS40 3.6 9.8 1.0 CA A:HIS40 3.7 9.6 1.0 O A:GLY39 4.0 12.7 1.0 CG A:MET86 4.0 9.9 1.0 NE2 A:HIS40 4.1 12.5 1.0 NE2 A:HIS81 4.1 14.7 1.0 CD2 A:HIS81 4.2 13.8 1.0 CD2 A:HIS40 4.2 11.8 1.0 N A:HIS81 4.4 12.6 1.0 CB A:MET86 4.5 9.3 1.0 CG A:PRO80 4.5 13.4 1.0 N A:HIS40 4.5 10.5 1.0 CA A:HIS81 4.5 11.5 1.0 C A:GLY39 4.5 12.2 1.0 CA A:CYS78 4.6 9.6 1.0 N A:ASN41 4.7 8.4 1.0 C A:HIS40 4.8 9.0 1.0 CD A:PRO80 4.9 13.1 1.0 CD1 A:PHE16 5.0 14.0 1.0

Copper binding site 2 out of 2 in the Pseudoazurin M16F


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Pseudoazurin M16F within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu125 b:11.2 occ:1.00 ND1 B:HIS40 2.1 10.7 1.0 ND1 B:HIS81 2.1 10.7 1.0 SG B:CYS78 2.2 9.2 1.0 SD B:MET86 2.7 9.3 1.0 CE1 B:HIS40 3.0 9.4 1.0 CE1 B:HIS81 3.0 12.5 1.0 CG B:HIS81 3.1 10.3 1.0 CG B:HIS40 3.1 9.2 1.0 CB B:CYS78 3.2 7.9 1.0 CB B:HIS81 3.4 9.8 1.0 CE B:MET86 3.4 10.2 1.0 CB B:HIS40 3.5 8.9 1.0 CA B:HIS40 3.6 9.2 1.0 O B:GLY39 4.0 11.6 1.0 CG B:MET86 4.1 7.9 1.0 NE2 B:HIS40 4.1 8.0 1.0 NE2 B:HIS81 4.2 11.8 1.0 CD2 B:HIS81 4.2 12.1 1.0 CD2 B:HIS40 4.2 7.6 1.0 N B:HIS81 4.4 10.3 1.0 N B:HIS40 4.4 9.6 1.0 CG B:PRO80 4.4 11.6 1.0 C B:GLY39 4.5 11.0 1.0 CA B:HIS81 4.5 9.6 1.0 CB B:MET86 4.6 6.8 1.0 CA B:CYS78 4.6 8.0 1.0 N B:ASN41 4.7 7.9 1.0 C B:HIS40 4.8 9.1 1.0 CD2 B:PHE16 5.0 7.6 1.0

S.Yanagisawa, P.B.Crowley, S.J.Firbank, A.T.Lawler, D.M.Hunter, W.Mcfarlane, C.Li, T.Kohzuma, M.J.Banfield, C.Dennison. Pi-Interaction Tuning of the Active Site Properties of Metalloproteins. J.Am.Chem.Soc. V. 130 15420 2008.
ISSN: ISSN 0002-7863
PubMed: 18939838
DOI: 10.1021/JA8038135