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Copper in PDB 9csv: Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, Oxidized By Hydrogen Peroxide

Protein crystallography data

The structure of Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, Oxidized By Hydrogen Peroxide, PDB code: 9csv was solved by K.S.Uyeda, A.H.Follmer, A.S.Borovik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.38 / 1.60
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 57.55, 57.55, 177.73, 90, 90, 90
R / Rfree (%) 20.6 / 23.4

Copper Binding Sites:

The binding sites of Copper atom in the Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, Oxidized By Hydrogen Peroxide (pdb code 9csv). 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 Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, Oxidized By Hydrogen Peroxide, PDB code: 9csv:

Copper binding site 1 out of 1 in 9csv

Go back to Copper Binding Sites List in 9csv
Copper binding site 1 out of 1 in the Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, Oxidized By Hydrogen Peroxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, Oxidized By Hydrogen Peroxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:36.0
occ:0.76
N4 A:QG7201 1.9 36.7 1.0
N5 A:QG7201 2.0 37.3 1.0
N3 A:QG7201 2.1 30.1 1.0
OD1 A:ASN49 2.4 41.5 0.5
O A:HOH372 2.5 47.2 1.0
C12 A:QG7201 2.7 39.1 1.0
C11 A:QG7201 2.8 30.0 1.0
C18 A:QG7201 2.9 39.8 1.0
C16 A:QG7201 2.9 47.3 1.0
C17 A:QG7201 2.9 36.1 1.0
H23 A:QG7201 2.9 39.1 1.0
C22 A:QG7201 3.0 47.7 1.0
H5 A:QG7201 3.1 36.0 1.0
H28 A:QG7201 3.1 56.8 1.0
C23 A:QG7201 3.1 33.2 1.0
H30 A:QG7201 3.1 57.2 1.0
H3 A:QG7201 3.2 43.3 1.0
H26 A:QG7201 3.3 39.8 1.0
C24 A:QG7201 3.5 32.5 1.0
CG A:ASN49 3.6 36.0 0.5
H6 A:QG7201 3.8 36.0 1.0
H4 A:QG7201 3.9 43.3 1.0
C13 A:QG7201 4.0 37.1 1.0
H22 A:QG7201 4.1 39.1 1.0
H25 A:QG7201 4.1 39.8 1.0
C15 A:QG7201 4.2 49.3 1.0
C19 A:QG7201 4.2 43.4 1.0
ND2 A:ASN49 4.2 38.2 0.5
C21 A:QG7201 4.3 44.6 1.0
C14 A:QG7201 4.6 42.2 1.0
N6 A:QG7201 4.7 29.8 1.0
CB A:ASN49 4.7 35.8 0.5
CB A:ASN49 4.8 35.8 0.5
ND2 A:ASN49 4.8 40.0 0.5
H29 A:QG7201 4.8 44.5 1.0
C20 A:QG7201 4.9 43.0 1.0
O1 A:QG7201 5.0 25.9 1.0

Reference:

K.S.Uyeda, A.H.Follmer, A.S.Borovik. Selective Oxidation of Active Site Aromatic Residues in Engineered Cu Proteins Chem Sci 2024.
ISSN: ESSN 2041-6539
DOI: 10.1039/D4SC06667G
Page generated: Mon Jul 14 09:51:57 2025

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