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Copper in PDB 4w7d: Crystal Structure of Full-Length Split Gfp Mutant D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group

Protein crystallography data

The structure of Crystal Structure of Full-Length Split Gfp Mutant D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group, PDB code: 4w7d 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) 66.57 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.420, 82.050, 113.870, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 22.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group (pdb code 4w7d). 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/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group, PDB code: 4w7d:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 4w7d

Go back to Copper Binding Sites List in 4w7d
Copper binding site 1 out of 3 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 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 D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:42.5
occ:1.00
NZ A:LYS3 2.5 51.1 0.6
CE A:LYS3 2.8 32.2 0.6
O A:HOH414 3.6 38.6 1.0
CD A:LYS3 4.3 30.5 0.6
O A:HOH561 4.5 48.6 1.0

Copper binding site 2 out of 3 in 4w7d

Go back to Copper Binding Sites List in 4w7d
Copper binding site 2 out of 3 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 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 D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:40.0
occ:1.00
ND1 A:HIS26 2.0 31.6 1.0
NE2 A:HIS21 2.3 37.5 1.0
O A:HOH401 2.9 47.0 1.0
CD2 A:HIS21 3.0 35.0 1.0
CG A:HIS26 3.0 33.6 1.0
CE1 A:HIS26 3.0 33.8 1.0
CB A:HIS26 3.3 27.2 1.0
CE1 A:HIS21 3.3 34.9 1.0
NE2 A:HIS26 4.1 41.9 1.0
CG A:HIS21 4.1 33.6 1.0
CD2 A:HIS26 4.2 38.0 1.0
CA A:HIS26 4.3 26.4 1.0
ND1 A:HIS21 4.3 32.7 1.0
OD1 A:ASP19 4.5 59.7 1.0
O A:GLY20 4.8 25.0 1.0
O A:HOH431 4.9 57.6 1.0

Copper binding site 3 out of 3 in 4w7d

Go back to Copper Binding Sites List in 4w7d
Copper binding site 3 out of 3 in the Crystal Structure of Full-Length Split Gfp Mutant D21H/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group


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/K26H with Copper Mediated Crystal Contacts, P 21 21 21 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:46.7
occ:1.00
NE2 A:HIS26 2.0 41.9 1.0
CE1 A:HIS26 2.7 33.8 1.0
O A:HOH432 2.8 55.2 1.0
CD2 A:HIS26 3.2 38.0 1.0
ND1 A:HIS26 3.9 31.6 1.0
CG A:HIS26 4.2 33.6 1.0
O A:GLY24 4.5 45.8 1.0
O A:HOH431 4.6 57.6 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: Mon Jul 14 04:08:01 2025

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