Cadmium in PDB 1pew: High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto

The structure of High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto, PDB code: 1pew was solved by C.Dealwis, V.Gupta, M.Wilkerson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.60
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	73.577, 73.577, 92.298, 90.00, 90.00, 90.00
R / Rfree (%)	25.2 / 27.3

The binding sites of Cadmium atom in the High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto (pdb code 1pew). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 4 binding sites of Cadmium where determined in the High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto, PDB code: 1pew:
Jump to Cadmium binding site number: 1; 2; 3; 4;

Cadmium binding site 1 out of 4 in the High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd901 b:29.9 occ:1.00 OD2 A:ASP85 2.3 4.6 1.0 OD1 A:ASP85 2.4 2.6 1.0 O A:HOH903 2.4 17.6 1.0 O A:HOH904 2.6 19.1 1.0 CG A:ASP85 2.7 6.5 1.0 O A:HOH905 2.9 29.3 1.0 CB A:ASP85 4.3 5.7 1.0 CB A:ARG103 4.3 9.0 1.0 CD A:ARG103 4.4 14.7 1.0 O A:HOH907 4.5 23.8 1.0 O A:HOH938 4.7 29.7 1.0 CG A:ARG103 4.8 11.4 1.0

Cadmium binding site 2 out of 4 in the High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd902 b:31.4 occ:1.00 O B:HOH911 2.1 28.3 1.0 O B:HOH918 2.2 21.3 1.0 OE2 B:GLU50 2.3 3.9 1.0 O B:HOH950 2.3 35.9 1.0 OE1 B:GLU50 2.5 7.2 1.0 CD B:GLU50 2.7 7.1 1.0 CG B:GLU50 4.2 7.5 1.0 CE2 B:TYR49 4.4 8.3 1.0 O B:HOH935 4.4 24.2 1.0 CD2 B:TYR49 5.0 8.7 1.0

Cadmium binding site 3 out of 4 in the High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd903 b:32.2 occ:1.00 O B:HOH913 1.8 29.4 1.0 OD1 B:ASP60 2.2 9.1 1.0 O B:HOH941 2.3 29.5 1.0 O B:HOH938 2.3 28.1 1.0 O B:HOH916 2.6 28.8 1.0 CG B:ASP60 3.0 10.0 1.0 OD2 B:ASP60 3.1 12.0 1.0 NE B:ARG54 4.4 8.5 1.0 CB B:ASP60 4.4 9.9 1.0 NH2 B:ARG54 4.5 8.6 1.0 CZ B:ARG54 5.0 10.6 1.0 CA B:ASP60 5.0 9.5 1.0

Cadmium binding site 4 out of 4 in the High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of High Resolution Crystal Structure of JTO2, A Mutant of the Non- Amyloidogenic LAMBA6 Light Chain, Jto within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd904 b:29.1 occ:1.00 OD1 B:ASP85 2.5 10.9 1.0 OD2 B:ASP85 2.5 10.7 1.0 CG B:ASP85 2.8 11.6 1.0 OH B:TYR87 3.7 16.7 1.0 O B:HOH920 4.3 42.2 1.0 CB B:ASP85 4.3 11.4 1.0 O B:HOH907 4.4 30.1 1.0 CZ B:TYR87 4.9 15.5 1.0

J.S.Wall, V.Gupta, M.Wilkerson, M.Schell, R.Loris, P.Adams, A.Solomon, F.Stevens, C.Dealwis. Structural Basis of Light Chain Amyloidogenicity: Comparison of the Thermodynamic Properties, Fibrillogenic Potential and Tertiary Structural Features of Four V(Lambda)6 Proteins J.Mol.Recog. V. 17 323 2004.
ISSN: ISSN 0952-3499
PubMed: 15227639
DOI: 10.1002/JMR.681