Copper in PDB 9csw: Streptavidin-E101Q-S112A-K121Y Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor

The structure of Streptavidin-E101Q-S112A-K121Y Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, PDB code: 9csw 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)	42.08 / 1.30
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	57.77, 57.77, 184.25, 90, 90, 90
R / Rfree (%)	16.6 / 18.9

The binding sites of Copper atom in the Streptavidin-E101Q-S112A-K121Y Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor (pdb code 9csw). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Streptavidin-E101Q-S112A-K121Y Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor, PDB code: 9csw:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Streptavidin-E101Q-S112A-K121Y 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-S112A-K121Y Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu202 b:76.0 occ:0.71 NE2 A:HIS87 2.5 20.2 1.0 O A:HOH382 2.8 36.6 1.0 CD2 A:HIS87 3.4 20.8 1.0 CE1 A:HIS87 3.5 19.1 1.0 O A:HOH325 4.3 37.4 1.0 CG A:HIS87 4.6 19.5 1.0 ND1 A:HIS87 4.6 19.3 1.0 O A:ASN85 4.7 20.7 1.0

Copper binding site 2 out of 2 in the Streptavidin-E101Q-S112A-K121Y 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 2 of Streptavidin-E101Q-S112A-K121Y Bound to Cu(II)-Biotin-Ethyl- Dipicolylamine Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu204 b:37.5 occ:1.00 N5 A:QG7201 1.9 28.2 1.0 N4 A:QG7201 2.0 33.0 1.0 OXT A:ACY203 2.1 29.6 1.0 N3 A:QG7201 2.1 30.3 1.0 O A:HOH381 2.6 48.0 1.0 C12 A:QG7201 2.6 34.0 1.0 C11 A:QG7201 2.6 32.8 1.0 H22 A:QG7201 2.7 30.6 1.0 C A:ACY203 2.7 25.5 1.0 H5 A:QG7201 2.8 39.4 1.0 C22 A:QG7201 2.8 31.4 1.0 O A:ACY203 2.8 30.2 1.0 C18 A:QG7201 2.8 28.9 1.0 H30 A:QG7201 2.9 37.7 1.0 C16 A:QG7201 3.0 35.5 1.0 C17 A:QG7201 3.0 30.1 1.0 C23 A:QG7201 3.2 28.3 1.0 H28 A:QG7201 3.2 42.6 1.0 C24 A:QG7201 3.3 25.5 1.0 H3 A:QG7201 3.5 36.1 1.0 H25 A:QG7201 3.6 34.0 1.0 H23 A:QG7201 3.6 30.6 1.0 H6 A:QG7201 3.7 39.4 1.0 H4 A:QG7201 3.9 36.1 1.0 C13 A:QG7201 4.0 35.1 1.0 H26 A:QG7201 4.1 34.0 1.0 C21 A:QG7201 4.1 30.6 1.0 C19 A:QG7201 4.2 29.0 1.0 C15 A:QG7201 4.2 36.7 1.0 CH3 A:ACY203 4.2 26.7 1.0 C14 A:QG7201 4.6 37.1 1.0 O1 A:QG7201 4.7 19.7 1.0 N6 A:QG7201 4.7 23.0 1.0 C20 A:QG7201 4.7 30.0 1.0 H29 A:QG7201 4.8 42.1 1.0 H31 A:QG7201 4.9 36.8 1.0 H33 A:QG7201 5.0 34.8 1.0

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