Copper in PDB 4w7c: Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group

The structure of Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group, PDB code: 4w7c was solved by D.J.Leibly, G.S.Waldo, T.O.Yeates, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	96.15 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	205.490, 69.420, 102.810, 90.00, 110.73, 90.00
R / Rfree (%)	22.7 / 25.4

The binding sites of Copper atom in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group (pdb code 4w7c). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group, PDB code: 4w7c:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group


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 Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:0.5 occ:1.00 NE2 A:HIS21 2.0 91.2 1.0 NE2 B:HIS21 2.1 84.4 1.0 CE1 A:HIS21 2.4 90.6 1.0 OD2 B:ASP19 2.8 0.5 1.0 OD1 B:ASP19 2.9 0.1 1.0 CE1 B:HIS21 2.9 84.0 1.0 CG B:ASP19 3.1 99.8 1.0 CD2 B:HIS21 3.1 83.0 1.0 CD2 A:HIS21 3.2 93.6 1.0 ND1 A:HIS21 3.6 93.0 1.0 CG A:ASP19 3.7 0.6 1.0 OD2 A:ASP19 3.9 0.1 1.0 OD1 A:ASP19 3.9 0.9 1.0 CG A:HIS21 4.0 92.5 1.0 ND1 B:HIS21 4.0 83.5 1.0 CB A:ASP19 4.1 97.3 1.0 CG B:HIS21 4.2 82.3 1.0 CB B:ASP19 4.3 93.3 1.0 SG B:CYS26 4.6 0.5 1.0 CA A:ASP19 4.8 91.2 1.0 CA B:ASP19 5.0 87.0 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group


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 Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, C 2 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu301 b:0.7 occ:1.00 NE2 C:HIS21 2.0 0.5 1.0 NE2 D:HIS21 2.1 99.6 1.0 OD1 D:ASP19 2.4 0.3 1.0 CE1 C:HIS21 2.6 0.7 1.0 CE1 D:HIS21 2.8 98.3 1.0 OD2 D:ASP19 2.9 0.8 1.0 CG D:ASP19 3.0 0.6 1.0 CD2 C:HIS21 3.1 0.4 1.0 CD2 D:HIS21 3.3 98.7 1.0 ND1 C:HIS21 3.8 0.7 1.0 CG C:ASP19 3.8 0.7 1.0 OD1 C:ASP19 3.9 0.7 1.0 CG C:HIS21 4.0 0.4 1.0 ND1 D:HIS21 4.0 98.4 1.0 CB C:ASP19 4.1 0.3 1.0 OD2 C:ASP19 4.2 0.1 1.0 CG D:HIS21 4.3 98.6 1.0 CB D:ASP19 4.5 0.3 1.0 CA C:ASP19 4.6 0.9 1.0 N C:GLY20 4.7 0.8 1.0 C C:ASP19 4.8 0.1 1.0 O C:GLY20 4.8 0.4 1.0

D.J.Leibly, M.A.Arbing, I.Pashkov, N.Devore, G.S.Waldo, T.C.Terwilliger, T.O.Yeates. Engineering Novel Oligomeric Gfp Molecules For Synthetic Symmetrization Applications To Be Published.