Cadmium in PDB 2mrt: Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy

The binding sites of Cadmium atom in the Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy (pdb code 2mrt). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 3 binding sites of Cadmium where determined in the Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy, PDB code: 2mrt:
Jump to Cadmium binding site number: 1; 2; 3;

Cadmium binding site 1 out of 3 in the Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd102 b:0.6 occ:1.00 SG A:CYS29 2.5 1.0 1.0 SG A:CYS24 2.5 0.6 1.0 SG A:CYS19 2.5 1.6 1.0 SG A:CYS15 2.7 1.8 1.0 CB A:CYS15 3.3 1.4 1.0 CB A:CYS29 3.3 1.4 1.0 CB A:CYS24 3.4 0.6 1.0 CB A:CYS19 3.4 1.3 1.0 H A:ALA16 3.4 3.2 1.0 O A:CYS29 3.7 1.8 1.0 N A:ALA16 4.1 2.3 1.0 CD A:CD104 4.2 0.5 1.0 CD A:CD103 4.2 1.1 1.0 HA A:ALA16 4.5 3.5 1.0 CA A:CYS29 4.5 1.3 1.0 C A:CYS29 4.5 1.6 1.0 CB A:CYS21 4.5 0.8 1.0 H A:CYS26 4.6 2.1 1.0 CA A:CYS15 4.6 1.3 1.0 SG A:CYS7 4.6 0.7 1.0 H A:CYS21 4.7 0.9 1.0 C A:CYS15 4.8 1.4 1.0 CA A:CYS24 4.8 0.9 1.0 SG A:CYS21 4.9 0.8 1.0 CA A:CYS19 4.9 1.1 1.0 CA A:ALA16 4.9 2.7 1.0

Cadmium binding site 2 out of 3 in the Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd103 b:1.1 occ:1.00 SG A:CYS13 2.5 1.7 1.0 SG A:CYS15 2.5 1.8 1.0 SG A:CYS26 2.5 1.6 1.0 SG A:CYS7 2.6 0.7 1.0 H A:CYS15 3.2 1.5 1.0 CB A:CYS7 3.3 0.5 1.0 CB A:CYS15 3.3 1.4 1.0 CB A:CYS13 3.4 1.1 1.0 CB A:CYS26 3.4 1.6 1.0 N A:CYS15 4.1 1.3 1.0 SG A:CYS24 4.1 0.6 1.0 CD A:CD102 4.2 0.6 1.0 CD A:CD104 4.2 0.5 1.0 CA A:CYS15 4.3 1.3 1.0 CA A:CYS13 4.7 1.0 1.0 CA A:CYS7 4.8 0.6 1.0 C A:CYS13 4.8 1.1 1.0 H A:SER14 4.8 2.4 1.0 N A:SER14 4.8 1.7 1.0 CA A:CYS26 4.9 1.6 1.0 HA A:CYS7 4.9 0.7 1.0

Cadmium binding site 3 out of 3 in the Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd104 b:0.5 occ:1.00 SG A:CYS21 2.5 0.8 1.0 SG A:CYS5 2.5 0.6 1.0 SG A:CYS7 2.5 0.7 1.0 SG A:CYS24 2.6 0.6 1.0 H A:CYS7 3.2 0.7 1.0 CB A:CYS5 3.2 0.7 1.0 H A:SER6 3.3 0.8 1.0 CB A:CYS7 3.3 0.5 1.0 HA A:CYS5 3.3 0.9 1.0 CB A:CYS24 3.3 0.6 1.0 CB A:CYS21 3.4 0.8 1.0 HA A:CYS24 3.5 1.0 1.0 CA A:CYS5 3.7 0.8 1.0 N A:CYS7 3.7 0.7 1.0 N A:SER6 3.9 0.8 1.0 CA A:CYS24 4.0 0.9 1.0 CA A:CYS7 4.1 0.6 1.0 C A:CYS5 4.2 0.9 1.0 CD A:CD102 4.2 0.6 1.0 CD A:CD103 4.2 1.1 1.0 SG A:CYS19 4.4 1.6 1.0 H A:LYS25 4.4 1.2 1.0 HA A:CYS7 4.5 0.7 1.0 C A:SER6 4.6 0.8 1.0 SG A:CYS26 4.6 1.6 1.0 CA A:SER6 4.9 0.9 1.0 CA A:CYS21 4.9 0.8 1.0 N A:CYS24 5.0 1.0 1.0

P.Schultze, E.Worgotter, W.Braun, G.Wagner, M.Vasak, J.H.Kagi, K.Wuthrich. Conformation of [CD7]-Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy. J.Mol.Biol. V. 203 251 1988.
ISSN: ISSN 0022-2836
PubMed: 3184190
DOI: 10.1016/0022-2836(88)90106-4