Copper in PDB 4r0o: Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution

The structure of Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution, PDB code: 4r0o was solved by G.Cattani, L.Vogeley, P.B.Crowley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.03 / 4.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	116.140, 116.140, 172.140, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 27

The binding sites of Copper atom in the Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution (pdb code 4r0o). 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 Pegylated Plastocyanin at 4.2 A Resolution, PDB code: 4r0o:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution


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 Pegylated Plastocyanin at 4.2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:0.0 occ:1.00 ND1 A:HIS39 1.9 0.9 1.0 ND1 A:HIS92 2.0 0.6 1.0 SD A:MET97 2.3 0.7 1.0 SG A:CYS89 2.4 0.5 1.0 CE1 A:HIS39 2.6 0.5 1.0 CE1 A:HIS92 2.7 0.5 1.0 CG A:HIS92 3.1 0.9 1.0 CB A:CYS89 3.1 0.5 1.0 CG A:HIS39 3.1 0.3 1.0 CE A:MET97 3.2 0.8 1.0 CB A:HIS92 3.6 0.4 1.0 CB A:HIS39 3.7 0.6 1.0 NE2 A:HIS39 3.8 0.9 1.0 NE2 A:HIS92 3.9 0.0 1.0 CG A:MET97 3.9 0.6 1.0 CD2 A:HIS92 4.0 0.3 1.0 CD2 A:HIS39 4.1 0.7 1.0 CA A:HIS39 4.1 0.8 1.0 O A:PRO38 4.1 0.8 1.0 CB A:MET97 4.4 0.1 1.0 CA A:CYS89 4.6 0.8 1.0 N A:HIS92 4.7 0.6 1.0 CD2 A:LEU14 4.7 0.9 1.0 CA A:HIS92 4.8 0.5 1.0 C A:PRO38 4.9 0.7 1.0 N A:HIS39 4.9 0.6 1.0

Copper binding site 2 out of 4 in the Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution


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 Pegylated Plastocyanin at 4.2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:0.8 occ:1.00 ND1 B:HIS39 1.9 77.7 1.0 ND1 B:HIS92 2.0 0.3 1.0 SD B:MET97 2.2 0.8 1.0 SG B:CYS89 2.3 0.1 1.0 CE1 B:HIS39 2.6 84.2 1.0 CE1 B:HIS92 2.9 0.6 1.0 CB B:CYS89 2.9 0.6 1.0 CG B:HIS92 3.1 0.5 1.0 CE B:MET97 3.1 0.6 1.0 CG B:HIS39 3.1 82.4 1.0 CB B:HIS92 3.6 0.3 1.0 CB B:HIS39 3.8 89.3 1.0 CG B:MET97 3.8 0.3 1.0 NE2 B:HIS39 3.8 85.8 1.0 NE2 B:HIS92 4.0 0.7 1.0 CD2 B:HIS39 4.1 85.1 1.0 CD2 B:HIS92 4.1 0.8 1.0 CA B:HIS39 4.2 96.2 1.0 O B:PRO38 4.2 95.5 1.0 CB B:MET97 4.3 0.3 1.0 CA B:CYS89 4.4 0.3 1.0 N B:HIS92 4.7 1.0 1.0 CA B:HIS92 4.7 0.1 1.0 CD2 B:LEU14 4.8 0.6 1.0 C B:PRO38 5.0 0.3 1.0 N B:HIS39 5.0 0.7 1.0

Copper binding site 3 out of 4 in the Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution


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 Pegylated Plastocyanin at 4.2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu201 b:1.0 occ:1.00 ND1 C:HIS92 2.0 0.6 1.0 ND1 C:HIS39 2.1 96.6 1.0 SG C:CYS89 2.2 0.2 1.0 SD C:MET97 2.4 0.4 1.0 CB C:CYS89 2.8 0.4 1.0 CE1 C:HIS92 2.8 0.2 1.0 CE1 C:HIS39 2.8 99.2 1.0 CG C:HIS92 3.0 0.8 1.0 CG C:HIS39 3.3 99.2 1.0 CE C:MET97 3.3 99.6 1.0 CB C:HIS92 3.4 0.5 1.0 CB C:HIS39 3.8 0.4 1.0 CG C:MET97 3.9 0.0 1.0 NE2 C:HIS92 4.0 0.8 1.0 NE2 C:HIS39 4.1 95.2 1.0 CD2 C:HIS92 4.1 0.0 1.0 CA C:HIS39 4.1 0.5 1.0 O C:PRO38 4.2 0.2 1.0 CD2 C:HIS39 4.3 93.6 1.0 CB C:MET97 4.3 1.0 1.0 CA C:CYS89 4.3 0.9 1.0 N C:HIS92 4.4 0.8 1.0 CA C:HIS92 4.6 0.8 1.0 C C:CYS89 4.8 98.0 1.0 CD2 C:LEU14 4.9 1.0 1.0 C C:PRO38 4.9 0.6 1.0 N C:HIS39 5.0 0.4 1.0

Copper binding site 4 out of 4 in the Crystal Structure of Pegylated Plastocyanin at 4.2 A Resolution


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 Pegylated Plastocyanin at 4.2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu201 b:0.8 occ:1.00 ND1 D:HIS39 2.0 87.5 1.0 ND1 D:HIS92 2.0 0.3 1.0 SG D:CYS89 2.2 0.5 1.0 SD D:MET97 2.3 0.8 1.0 CE1 D:HIS39 2.7 91.8 1.0 CE1 D:HIS92 2.9 0.8 1.0 CB D:CYS89 2.9 0.6 1.0 CG D:HIS92 3.0 0.9 1.0 CG D:HIS39 3.2 91.2 1.0 CE D:MET97 3.2 0.9 1.0 CB D:HIS92 3.5 0.4 1.0 CB D:HIS39 3.8 0.0 1.0 CG D:MET97 3.8 0.5 1.0 NE2 D:HIS39 3.9 92.8 1.0 NE2 D:HIS92 4.0 0.0 1.0 CD2 D:HIS92 4.1 0.0 1.0 CD2 D:HIS39 4.1 91.4 1.0 CA D:HIS39 4.2 1.0 1.0 CB D:MET97 4.2 0.1 1.0 O D:PRO38 4.3 0.2 1.0 CA D:CYS89 4.4 0.7 1.0 N D:HIS92 4.5 0.9 1.0 CA D:HIS92 4.6 0.4 1.0 CD2 D:LEU14 4.7 0.6 1.0 C D:CYS89 5.0 94.6 1.0

G.Cattani, L.Vogeley, P.B.Crowley. Structure of A Pegylated Protein Reveals A Highly Porous Double-Helical Assembly. Nat.Chem. V. 7 823 2015.
ISSN: ISSN 1755-4330
PubMed: 26391082
DOI: 10.1038/NCHEM.2342