Copper in PDB 3t56: Crystal Structure of the Pre-Extrusion State of the Cusba Adaptor- Transporter Complex

The structure of Crystal Structure of the Pre-Extrusion State of the Cusba Adaptor- Transporter Complex, PDB code: 3t56 was solved by C.-C.Su, F.Long, E.W.Yu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.25 / 3.42
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	160.121, 160.121, 684.945, 90.00, 90.00, 120.00
R / Rfree (%)	25.9 / 29.4

The binding sites of Copper atom in the Crystal Structure of the Pre-Extrusion State of the Cusba Adaptor- Transporter Complex (pdb code 3t56). 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 Crystal Structure of the Pre-Extrusion State of the Cusba Adaptor- Transporter Complex, PDB code: 3t56:

Copper binding site 1 out of 1 in the Crystal Structure of the Pre-Extrusion State of the Cusba Adaptor- Transporter Complex


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Pre-Extrusion State of the Cusba Adaptor- Transporter Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1048 b:0.1 occ:1.00 SD A:MET623 2.7 0.4 1.0 SD A:MET573 2.8 86.5 1.0 CE A:MET672 2.8 0.1 0.8 SD A:MET672 2.8 0.0 0.2 CE A:MET573 3.0 90.8 1.0 OE2 A:GLU625 3.2 96.1 1.0 CE A:MET623 3.9 0.6 1.0 CG A:MET672 4.0 0.4 0.2 CE A:MET672 4.0 0.7 0.2 CG A:MET623 4.0 0.1 1.0 CG A:MET573 4.1 65.3 1.0 SD A:MET672 4.2 0.1 0.8 CD A:GLU625 4.2 79.2 1.0 ND2 A:ASN668 4.2 0.0 0.2 CB A:LYS678 4.3 0.8 0.8 CD A:LYS678 4.3 77.1 0.8 CG A:GLU625 4.4 73.2 1.0 CB A:ALA619 4.7 60.4 1.0 OD1 A:ASN668 4.9 89.3 0.2 OD1 A:ASN668 4.9 0.3 0.8 CG A:LYS678 5.0 86.2 0.8

C.C.Su, F.Long, H.T.Lei, J.R.Bolla, S.V.Do, K.R.Rajashankar, E.W.Yu. Charged Amino Acids (R83, E567, D617, E625, R669, and K678) of Cusa Are Required For Metal Ion Transport in the Cus Efflux System. J.Mol.Biol. V. 422 429 2012.
ISSN: ISSN 0022-2836
PubMed: 22683351
DOI: 10.1016/J.JMB.2012.05.038