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Copper in PDB 6x8x: Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1

Protein crystallography data

The structure of Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1, PDB code: 6x8x was solved by F.A.Tezcan, A.Kakkis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.84 / 2.51
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.172, 82.172, 48.072, 90.00, 90.00, 120.00
R / Rfree (%) 28.5 / 34.2

Other elements in 6x8x:

The structure of Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1 also contains other interesting chemical elements:

Iron (Fe) 1 atom
Calcium (Ca) 5 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1 (pdb code 6x8x). 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 Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1, PDB code: 6x8x:

Copper binding site 1 out of 1 in 6x8x

Go back to Copper Binding Sites List in 6x8x
Copper binding site 1 out of 1 in the Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu-Bound Structure of An Engineered Metal-Dependent Protein Trimer, TRICYT1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:42.5
occ:0.45
NE2 A:HIS77 2.3 48.6 1.0
NE2 A:HIS73 2.4 39.2 1.0
CD2 A:HIS77 3.1 48.5 1.0
CD2 A:HIS73 3.1 33.1 1.0
CE1 A:HIS73 3.4 37.3 1.0
CE1 A:HIS77 3.4 49.2 1.0
CG A:HIS77 4.3 45.9 1.0
CG A:HIS73 4.3 32.6 1.0
ND1 A:HIS77 4.4 50.4 1.0
ND1 A:HIS73 4.4 32.1 1.0

Reference:

F.A.Tezcan, A.Kakkis, D.Gagnon, J.Esselborn, R.D.Britt. Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32830423
DOI: 10.1002/ANIE.202009226
Page generated: Sun Dec 13 11:26:45 2020

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