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Copper in PDB 5k68: Designed Artificial Cupredoxins

Protein crystallography data

The structure of Designed Artificial Cupredoxins, PDB code: 5k68 was solved by S.I.Mann, T.Heinisch, A.C.Weitz, M.R.Hendrich, T.R.Ward, A.S.Borovik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.90 / 1.40
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 57.690, 57.690, 183.610, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 18.1

Copper Binding Sites:

The binding sites of Copper atom in the Designed Artificial Cupredoxins (pdb code 5k68). 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 Designed Artificial Cupredoxins, PDB code: 5k68:

Copper binding site 1 out of 1 in 5k68

Go back to Copper Binding Sites List in 5k68
Copper binding site 1 out of 1 in the Designed Artificial Cupredoxins


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Designed Artificial Cupredoxins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:43.9
occ:0.80
CU1 A:SI9201 0.0 43.9 0.8
SG A:CYS112 2.1 22.8 1.0
N5 A:SI9201 2.1 72.3 0.8
N4 A:SI9201 2.1 60.8 0.8
N3 A:SI9201 2.3 42.5 0.8
C20 A:SI9201 2.7 66.6 0.8
CB A:CYS112 3.0 17.3 1.0
C17 A:SI9201 3.0 63.9 0.8
C13 A:SI9201 3.0 38.3 0.8
C24 A:SI9201 3.2 82.3 0.8
C18 A:SI9201 3.2 63.9 0.8
C19 A:SI9201 3.2 52.3 0.8
C11 A:SI9201 3.3 57.9 1.0
C26 A:SI9201 3.3 64.3 0.8
C12 A:SI9201 3.5 38.6 1.0
C25 A:SI9201 3.7 72.1 0.8
C21 A:SI9201 4.0 78.2 0.8
C14 A:SI9201 4.3 52.9 0.8
C16 A:SI9201 4.4 61.7 0.8
CA A:CYS112 4.4 12.9 1.0
C23 A:SI9201 4.5 82.7 0.8
C27 A:SI9201 4.5 25.2 1.0
C22 A:SI9201 4.7 0.6 0.8
C28 A:SI9201 4.9 21.1 1.0
C15 A:SI9201 4.9 38.3 0.8
N A:CYS112 4.9 11.7 1.0
O A:SER122 5.0 13.2 1.0

Reference:

S.I.Mann, T.Heinisch, A.C.Weitz, M.P.Hendrich, T.R.Ward, A.S.Borovik. Modular Artificial Cupredoxins. J.Am.Chem.Soc. V. 138 9073 2016.
ISSN: ESSN 1520-5126
PubMed: 27385206
DOI: 10.1021/JACS.6B05428
Page generated: Sun Dec 13 11:18:13 2020

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