Copper in PDB 4jfn: Crystal Structure of the N-Terminal, Growth Factor-Like Domain of the Amyloid Precursor Protein Bound to Copper

The structure of Crystal Structure of the N-Terminal, Growth Factor-Like Domain of the Amyloid Precursor Protein Bound to Copper, PDB code: 4jfn was solved by K.Wild, F.Baumkotter, S.Kins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.28 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.050, 49.070, 66.160, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 23

The binding sites of Copper atom in the Crystal Structure of the N-Terminal, Growth Factor-Like Domain of the Amyloid Precursor Protein Bound to Copper (pdb code 4jfn). 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 N-Terminal, Growth Factor-Like Domain of the Amyloid Precursor Protein Bound to Copper, PDB code: 4jfn:

Copper binding site 1 out of 1 in the Crystal Structure of the N-Terminal, Growth Factor-Like Domain of the Amyloid Precursor Protein Bound to Copper


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 N-Terminal, Growth Factor-Like Domain of the Amyloid Precursor Protein Bound to Copper within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:47.2 occ:0.60 NE2 A:HIS110 1.9 49.2 1.0 NE2 A:HIS108 2.0 52.1 1.0 CD2 A:HIS110 2.7 48.3 1.0 CD2 A:HIS108 3.0 49.8 1.0 CE1 A:HIS108 3.0 53.8 1.0 CE1 A:HIS110 3.1 51.3 1.0 NH2 A:ARG40 3.3 66.5 1.0 CG A:HIS110 3.9 46.4 1.0 ND1 A:HIS110 4.0 50.8 1.0 ND1 A:HIS108 4.1 52.1 1.0 CG A:HIS108 4.1 49.6 1.0 CZ A:ARG40 4.3 65.7 1.0 NH1 A:ARG40 4.9 66.8 1.0 OG1 A:THR107 4.9 61.5 1.0

F.Baumkotter, N.Schmidt, C.Vargas, S.Schilling, R.Weber, K.Wagner, S.Fiedler, W.Klug, J.Radzimanowski, S.Nickolaus, S.Keller, S.Eggert, K.Wild, S.Kins. Amyloid Precursor Protein Dimerization and Synaptogenic Function Depend on Copper Binding to the Growth Factor-Like Domain J.Neurosci. V. 34 11159 2014.
ISSN: ISSN 0270-6474
PubMed: 25122912
DOI: 10.1523/JNEUROSCI.0180-14.2014