Manganese in PDB 4ez1: Crystal Structure of Acetylcholine Binding Protein (Achbp) From Aplysia Californica in Complex with Alpha-Conotoxin Buia

The structure of Crystal Structure of Acetylcholine Binding Protein (Achbp) From Aplysia Californica in Complex with Alpha-Conotoxin Buia, PDB code: 4ez1 was solved by T.T.Talley, A.S.Reger, C.Kim, B.Sankaran, K.Ho, P.Taylor, J.M.Mcintosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 2.49
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.437, 78.636, 117.636, 90.00, 93.20, 90.00
R / Rfree (%)	17.1 / 22.7

The binding sites of Manganese atom in the Crystal Structure of Acetylcholine Binding Protein (Achbp) From Aplysia Californica in Complex with Alpha-Conotoxin Buia (pdb code 4ez1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Acetylcholine Binding Protein (Achbp) From Aplysia Californica in Complex with Alpha-Conotoxin Buia, PDB code: 4ez1:

Manganese binding site 1 out of 1 in the Crystal Structure of Acetylcholine Binding Protein (Achbp) From Aplysia Californica in Complex with Alpha-Conotoxin Buia


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Acetylcholine Binding Protein (Achbp) From Aplysia Californica in Complex with Alpha-Conotoxin Buia within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn301 b:31.6 occ:0.76 OD1 C:ASP-3 1.9 42.8 1.0 NE2 C:HIS1 2.0 55.0 1.0 OD2 C:ASP-3 2.2 44.5 1.0 CG C:ASP-3 2.2 41.7 1.0 CE1 C:HIS1 2.2 45.6 1.0 CD2 C:HIS1 3.3 56.1 1.0 ND1 C:HIS1 3.4 50.8 1.0 CB C:ASP-3 3.7 44.3 1.0 CG C:HIS1 3.9 51.7 1.0 O C:ASP-3 4.4 44.9 1.0 CA C:ASP-3 4.5 54.8 1.0 C C:ASP-3 4.7 48.3 1.0

O.M.Filchakova, T.T.Talley, A.S.Reger, C.Kim, K.Ho, K.Han, P.Taylor, J.M.Mcintosh. Pairwise Interaction of Alpha-Conotoxin Buia PRO6 with the Beta Subunit of Nicotinic Acetylcholine Receptor To Be Published.