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Copper in PDB 4w77: Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 3

Protein crystallography data

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 3, PDB code: 4w77 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) 60.79 / 3.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.120, 68.290, 121.580, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 29.1

Copper Binding Sites:

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 3 (pdb code 4w77). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was 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 3, PDB code: 4w77:

Copper binding site 1 out of 1 in 4w77

Go back to Copper Binding Sites List in 4w77
Copper binding site 1 out of 1 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 3


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 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:64.9
occ:1.00
NE2 A:HIS21 2.2 68.7 1.0
NE2 B:HIS21 2.2 75.0 1.0
OD1 B:ASP19 2.6 73.5 1.0
OD1 A:ASP19 2.9 68.8 1.0
CE1 A:HIS21 3.0 72.5 1.0
OD2 A:ASP19 3.1 70.0 1.0
CD2 B:HIS21 3.1 73.0 1.0
OD2 B:ASP19 3.2 72.9 1.0
CD2 A:HIS21 3.2 66.6 1.0
CG B:ASP19 3.3 72.3 1.0
CE1 B:HIS21 3.3 77.3 1.0
CG A:ASP19 3.3 68.4 1.0
SG B:CYS26 3.9 95.5 1.0
ND1 A:HIS21 4.1 72.9 1.0
CG A:HIS21 4.3 69.2 1.0
CG B:HIS21 4.3 74.2 1.0
ND1 B:HIS21 4.3 76.9 1.0
SG A:CYS26 4.6 0.2 1.0
CB A:ASP19 4.7 66.2 1.0
CB B:ASP19 4.7 70.2 1.0
O A:GLY20 4.9 64.8 1.0

Reference:

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.
Page generated: Sun Dec 13 11:16:06 2020

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