Copper in PDB 4w7a: Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4

The structure of Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4, PDB code: 4w7a 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)	96.28 / 3.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	120.830, 121.330, 192.560, 90.00, 90.00, 90.00
R / Rfree (%)	27.8 / 30.2

The binding sites of Copper atom in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4 (pdb code 4w7a). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4, PDB code: 4w7a:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4


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, P 21 21 21 Space Group, Form 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:98.9 occ:1.00 NE2 A:HIS21 2.1 0.2 1.0 NE2 B:HIS21 2.2 71.0 1.0 CE1 B:HIS21 2.3 71.4 1.0 OD1 B:ASP19 2.3 0.3 1.0 OD1 A:ASP19 2.5 0.4 1.0 CE1 A:HIS21 3.1 0.8 1.0 SG A:CYS26 3.1 0.4 1.0 CD2 A:HIS21 3.2 0.0 1.0 CG A:ASP19 3.3 1.0 1.0 CD2 B:HIS21 3.4 81.0 1.0 OD2 A:ASP19 3.4 0.6 1.0 CG B:ASP19 3.4 0.7 1.0 ND1 B:HIS21 3.4 85.3 1.0 OD2 B:ASP19 3.7 0.8 1.0 CG B:HIS21 4.0 76.8 1.0 ND1 A:HIS21 4.2 0.1 1.0 CG A:HIS21 4.3 0.9 1.0 O B:GLY20 4.5 93.8 1.0 SG B:CYS26 4.6 0.9 1.0 N B:GLY20 4.6 72.8 1.0 CB B:ASP19 4.7 0.3 1.0 CB A:ASP19 4.7 0.7 1.0 CB A:CYS26 4.9 0.2 1.0 C B:ASP19 4.9 98.5 1.0 C B:GLY20 4.9 81.8 1.0 CA B:ASP19 4.9 0.2 1.0 O A:GLY20 5.0 85.6 1.0

Copper binding site 2 out of 3 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4


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, P 21 21 21 Space Group, Form 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu302 b:0.5 occ:1.00 NE2 A:HIS25 3.2 0.3 1.0 CE1 A:HIS25 3.8 0.8 1.0 CD2 A:HIS25 4.4 0.8 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4


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 Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 4 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu301 b:0.3 occ:1.00 NE2 D:HIS21 2.1 1.0 1.0 CE1 D:HIS21 2.5 0.8 1.0 NE2 C:HIS21 2.6 93.9 1.0 CE1 C:HIS21 2.9 98.1 1.0 CD2 D:HIS21 3.2 99.2 1.0 ND1 D:HIS21 3.7 0.1 1.0 CD2 C:HIS21 3.8 92.2 1.0 CB C:ASP19 3.8 0.1 1.0 OD2 C:ASP19 4.0 0.9 1.0 CG D:HIS21 4.0 99.8 1.0 ND1 C:HIS21 4.2 97.6 1.0 SG C:CYS26 4.2 0.1 1.0 CG C:ASP19 4.4 0.7 1.0 CB D:ASP19 4.4 0.7 1.0 CG C:HIS21 4.6 93.8 1.0 O D:GLY20 4.6 0.9 1.0 N D:GLY20 4.7 0.3 1.0 CA D:ASP19 4.8 0.4 1.0 CB D:CYS26 4.8 0.9 1.0 C D:ASP19 4.9 0.8 1.0 CG D:ASP19 4.9 0.8 1.0 CA C:ASP19 4.9 0.6 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.