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Copper in PDB 9csu: Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor

Protein crystallography data

The structure of Streptavidin-E101Q-S112Y-K121A Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, PDB code: 9csu 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) 54.72 / 1.60
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 57.7, 57.7, 178.05, 90, 90, 90
R / Rfree (%) 17.5 / 20.7

Copper Binding Sites:

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

Copper binding site 1 out of 1 in 9csu

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


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu203

b:20.2
occ:0.65
N4 A:QG7202 1.9 29.5 1.0
N5 A:QG7202 2.0 36.3 1.0
N3 A:QG7202 2.1 27.8 1.0
OXT A:ACY201 2.3 56.5 0.9
OD1 A:ASN49 2.5 30.4 0.7
C12 A:QG7202 2.7 26.7 1.0
C18 A:QG7202 2.8 34.3 1.0
C16 A:QG7202 2.8 34.5 1.0
C11 A:QG7202 2.8 25.7 1.0
C17 A:QG7202 2.9 30.9 1.0
O A:HOH301 2.9 42.2 0.8
H28 A:QG7202 3.0 41.4 1.0
C22 A:QG7202 3.0 38.8 1.0
H23 A:QG7202 3.0 24.7 1.0
C A:ACY201 3.0 60.4 0.9
C23 A:QG7202 3.1 25.6 1.0
H30 A:QG7202 3.1 46.6 1.0
H5 A:QG7202 3.2 30.8 1.0
O A:ACY201 3.2 65.2 0.9
H3 A:QG7202 3.2 37.0 1.0
H26 A:QG7202 3.2 30.8 1.0
CG A:ASN49 3.5 27.7 0.7
C24 A:QG7202 3.5 20.6 1.0
H6 A:QG7202 3.8 30.8 1.0
H4 A:QG7202 3.8 37.0 1.0
ND2 A:ASN49 4.0 30.2 0.7
H25 A:QG7202 4.0 30.8 1.0
C13 A:QG7202 4.1 29.4 1.0
C15 A:QG7202 4.1 35.8 1.0
H22 A:QG7202 4.1 24.7 1.0
C19 A:QG7202 4.2 36.3 1.0
C21 A:QG7202 4.3 41.4 1.0
CH3 A:ACY201 4.5 60.0 0.9
C14 A:QG7202 4.6 31.2 1.0
H2 A:ACY201 4.7 72.0 0.9
N6 A:QG7202 4.7 19.2 1.0
CB A:ASN49 4.7 23.3 0.7
CB A:ASN49 4.8 21.9 0.3
C20 A:QG7202 4.8 40.4 1.0
H29 A:QG7202 4.9 35.2 1.0
H3 A:ACY201 4.9 72.0 0.9
H33 A:QG7202 5.0 43.5 1.0
H2 A:QG7202 5.0 42.9 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: Sun Dec 15 10:20:10 2024

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