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Copper in PDB 4w7r: Crystal Structure of Full-Length Split Gfp Mutant E124H/K126H Copper Mediated Dimer, P 21 Space Group

Protein crystallography data

The structure of Crystal Structure of Full-Length Split Gfp Mutant E124H/K126H Copper Mediated Dimer, P 21 Space Group, PDB code: 4w7r 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) 92.07 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 62.670, 87.190, 92.070, 90.00, 90.01, 90.00
R / Rfree (%) 22.3 / 25.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Full-Length Split Gfp Mutant E124H/K126H Copper Mediated Dimer, P 21 Space Group (pdb code 4w7r). 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 E124H/K126H Copper Mediated Dimer, P 21 Space Group, PDB code: 4w7r:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 4w7r

Go back to Copper Binding Sites List in 4w7r
Copper binding site 1 out of 2 in the Crystal Structure of Full-Length Split Gfp Mutant E124H/K126H Copper Mediated Dimer, P 21 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 E124H/K126H Copper Mediated Dimer, P 21 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:30.9
occ:1.00
NE2 A:HIS126 2.1 41.8 1.0
NE2 A:HIS124 2.1 35.2 1.0
NE2 B:HIS126 2.1 29.8 1.0
NE2 B:HIS124 2.1 34.2 1.0
CE1 A:HIS124 2.9 36.1 1.0
CE1 A:HIS126 3.0 40.3 1.0
CE1 B:HIS126 3.0 29.1 1.0
CD2 B:HIS124 3.1 33.9 1.0
CD2 A:HIS126 3.1 35.6 1.0
CE1 B:HIS124 3.1 40.0 1.0
CD2 B:HIS126 3.2 33.8 1.0
CD2 A:HIS124 3.2 38.0 1.0
ND1 A:HIS124 4.1 41.2 1.0
ND1 A:HIS126 4.1 40.7 1.0
ND1 B:HIS126 4.1 35.3 1.0
CG A:HIS126 4.2 34.2 1.0
CG B:HIS124 4.2 35.1 1.0
ND1 B:HIS124 4.2 33.4 1.0
CG A:HIS124 4.2 33.7 1.0
CG B:HIS126 4.3 35.2 1.0
O1 B:EDO302 4.7 54.2 1.0

Copper binding site 2 out of 2 in 4w7r

Go back to Copper Binding Sites List in 4w7r
Copper binding site 2 out of 2 in the Crystal Structure of Full-Length Split Gfp Mutant E124H/K126H Copper Mediated Dimer, P 21 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 E124H/K126H Copper Mediated Dimer, P 21 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu301

b:33.4
occ:1.00
NE2 D:HIS124 2.0 42.5 1.0
NE2 C:HIS124 2.1 45.8 1.0
NE2 C:HIS126 2.1 37.0 1.0
NE2 D:HIS126 2.1 50.0 1.0
CE1 D:HIS124 2.9 35.0 1.0
CE1 C:HIS124 3.0 44.3 1.0
CE1 D:HIS126 3.0 42.5 1.0
CE1 C:HIS126 3.0 27.6 1.0
CD2 C:HIS124 3.1 35.8 1.0
CD2 C:HIS126 3.1 31.7 1.0
CD2 D:HIS124 3.1 43.8 1.0
CD2 D:HIS126 3.1 28.8 1.0
ND1 D:HIS124 4.1 40.9 1.0
ND1 C:HIS124 4.1 39.9 1.0
ND1 D:HIS126 4.2 41.1 1.0
ND1 C:HIS126 4.2 33.6 1.0
CG C:HIS124 4.2 36.8 1.0
CG D:HIS124 4.2 35.8 1.0
CG C:HIS126 4.2 34.8 1.0
O D:HOH461 4.2 48.8 1.0
CG D:HIS126 4.2 27.7 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 11:16:10 2020

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