Zinc in PDB 3bkm: Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121)

The structure of Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121), PDB code: 3bkm was solved by L.A.Miles, K.S.Wun, G.A.Crespi, M.Fodero-Tavoletti, D.Galatis, C.J.Bageley, K.Beyreuther, C.L.Masters, R.Cappai, W.J.Mckinstry, K.J.Barnham, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.90 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.447, 90.496, 123.279, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 22.6

The structure of Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121) also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Zinc atom in the Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121) (pdb code 3bkm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121), PDB code: 3bkm:

Zinc binding site 1 out of 1 in the Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Anti-Amyloid-Beta Fab WO2 (Form A, P212121) within 5.0Å range: probe atom residue distance (Å) B Occ L:Zn216 b:22.9 occ:1.00 N L:ASP1 1.8 17.6 1.0 OD2 L:ASP1 2.2 19.0 1.0 O L:ASP1 2.2 17.8 1.0 CA L:ASP1 2.8 18.2 1.0 C L:ASP1 2.8 17.8 1.0 CG L:ASP1 3.2 19.3 1.0 CB L:ASP1 3.5 18.9 1.0 O L:HOH355 3.7 23.8 1.0 O L:HOH276 4.1 24.0 1.0 N L:VAL2 4.1 16.1 1.0 OD1 L:ASP1 4.3 21.3 1.0 O L:HOH331 4.4 25.8 1.0 CA L:VAL2 4.9 15.4 1.0

L.A.Miles, K.S.Wun, G.A.Crespi, M.T.Fodero-Tavoletti, D.Galatis, C.J.Bagley, K.Beyreuther, C.L.Masters, R.Cappai, W.J.Mckinstry, K.J.Barnham, M.W.Parker. Amyloid-Beta-Anti-Amyloid-Beta Complex Structure Reveals An Extended Conformation in the Immunodominant B-Cell Epitope. J.Mol.Biol. V. 377 181 2008.
ISSN: ISSN 0022-2836
PubMed: 18237744
DOI: 10.1016/J.JMB.2007.12.036