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Cadmium in PDB 1mrt: Conformation of Cd-7 Metallothionein-2 From Rat Liver in Aqueous Solution Determined By Nuclear Magnetic Resonance Spectroscopy

Cadmium Binding Sites:

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 1mrt). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 4 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: 1mrt:
Jump to Cadmium binding site number: 1; 2; 3; 4;

Cadmium binding site 1 out of 4 in 1mrt

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Cadmium binding site 1 out of 4 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:Cd101

b:1.0
occ:1.00
SG A:CYS57 2.5 2.8 1.0
SG A:CYS59 2.5 2.6 1.0
SG A:CYS50 2.6 1.7 1.0
SG A:CYS60 2.6 1.2 1.0
H A:CYS59 2.7 1.0 1.0
H A:CYS60 2.9 0.8 1.0
N A:CYS60 3.1 0.8 1.0
CB A:CYS59 3.3 0.9 1.0
CB A:CYS57 3.3 1.1 1.0
CB A:CYS50 3.3 1.4 1.0
CB A:CYS60 3.4 0.8 1.0
C A:CYS59 3.4 0.8 1.0
N A:CYS59 3.5 0.8 1.0
CA A:CYS59 3.6 0.8 1.0
CA A:CYS60 3.8 0.9 1.0
HA A:CYS50 4.0 1.1 1.0
H A:SER58 4.1 1.5 1.0
SG A:CYS37 4.2 1.1 1.0
O A:CYS59 4.2 0.9 1.0
H A:ALA61 4.2 2.8 1.0
CD A:CD106 4.3 1.4 1.0
CA A:CYS50 4.3 1.0 1.0
CD A:CD107 4.4 0.8 1.0
N A:SER58 4.5 0.8 1.0
HA A:CYS60 4.5 1.1 1.0
CA A:CYS57 4.6 1.2 1.0
HA A:CYS59 4.6 1.0 1.0
C A:SER58 4.8 0.9 1.0
C A:CYS57 4.8 1.6 1.0
N A:ALA61 4.9 2.0 1.0
C A:CYS60 4.9 1.4 1.0
O A:GLU52 4.9 2.5 1.0
HA A:CYS57 4.9 1.3 1.0

Cadmium binding site 2 out of 4 in 1mrt

Go back to Cadmium Binding Sites List in 1mrt
Cadmium binding site 2 out of 4 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:Cd105

b:1.2
occ:1.00
SG A:CYS34 2.5 0.9 1.0
HA A:CYS48 2.5 1.2 1.0
SG A:CYS48 2.5 1.2 1.0
SG A:CYS44 2.5 1.4 1.0
SG A:CYS33 2.6 2.4 1.0
CB A:CYS48 3.2 1.4 1.0
CA A:CYS48 3.3 1.2 1.0
CB A:CYS34 3.3 0.8 1.0
CB A:CYS44 3.3 1.1 1.0
CB A:CYS33 3.3 1.1 1.0
H A:CYS50 3.5 1.1 1.0
N A:CYS34 3.7 1.0 1.0
C A:CYS33 3.7 1.0 1.0
H A:CYS34 4.0 1.5 1.0
O A:CYS33 4.0 1.6 1.0
C A:CYS48 4.0 1.1 1.0
CA A:CYS34 4.1 1.0 1.0
CA A:CYS33 4.2 0.9 1.0
CB A:CYS50 4.2 1.4 1.0
H A:ILE49 4.2 1.7 1.0
O A:CYS50 4.3 1.5 1.0
CD A:CD107 4.3 0.8 1.0
N A:CYS50 4.3 1.0 1.0
N A:ILE49 4.4 1.1 1.0
N A:CYS48 4.4 1.3 1.0
CD A:CD106 4.4 1.4 1.0
HA A:CYS34 4.5 1.2 1.0
HA A:CYS44 4.6 1.8 1.0
CB A:CYS37 4.6 1.4 1.0
CA A:CYS44 4.6 1.3 1.0
O A:CYS37 4.7 2.1 1.0
CA A:CYS50 4.7 1.0 1.0
O A:CYS48 4.8 1.8 1.0
HA A:CYS33 4.8 1.2 1.0
H A:CYS48 4.8 2.5 1.0
C A:CYS50 5.0 1.0 1.0
H A:CYS37 5.0 1.0 1.0

Cadmium binding site 3 out of 4 in 1mrt

Go back to Cadmium Binding Sites List in 1mrt
Cadmium binding site 3 out of 4 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:Cd106

b:1.4
occ:1.00
SG A:CYS60 2.5 1.2 1.0
SG A:CYS44 2.5 1.4 1.0
SG A:CYS41 2.5 1.7 1.0
SG A:CYS37 2.8 1.1 1.0
CB A:CYS37 3.2 1.4 1.0
CB A:CYS44 3.3 1.1 1.0
CB A:CYS60 3.3 0.8 1.0
CB A:CYS41 3.4 1.2 1.0
CB A:CYS50 3.6 1.4 1.0
H A:CYS44 3.6 0.7 1.0
N A:CYS44 3.7 0.9 1.0
CB A:LYS43 4.1 2.4 1.0
CD A:CD107 4.1 0.8 1.0
CA A:CYS44 4.1 1.3 1.0
C A:LYS43 4.2 1.5 1.0
CD A:CD101 4.3 1.0 1.0
SG A:CYS50 4.3 1.7 1.0
SG A:CYS34 4.4 0.9 1.0
CD A:CD105 4.4 1.2 1.0
H A:LYS43 4.5 1.8 1.0
HA A:CYS44 4.5 1.8 1.0
CA A:LYS43 4.5 1.7 1.0
N A:LYS43 4.7 1.4 1.0
CA A:CYS41 4.7 1.1 1.0
CA A:CYS37 4.8 1.2 1.0
CA A:CYS60 4.8 0.9 1.0
O A:LYS43 4.8 2.1 1.0
CA A:CYS50 4.9 1.0 1.0
H A:CYS50 4.9 1.1 1.0
C A:CYS41 5.0 1.1 1.0

Cadmium binding site 4 out of 4 in 1mrt

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Cadmium binding site 4 out of 4 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 4 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:Cd107

b:0.8
occ:1.00
SG A:CYS36 2.5 1.9 1.0
SG A:CYS34 2.5 0.9 1.0
SG A:CYS37 2.5 1.1 1.0
SG A:CYS50 2.7 1.7 1.0
H A:CYS37 2.9 1.0 1.0
N A:CYS37 3.1 0.9 1.0
H A:CYS36 3.2 0.7 1.0
CB A:CYS36 3.2 0.8 1.0
CB A:CYS37 3.3 1.4 1.0
CB A:CYS50 3.4 1.4 1.0
CB A:CYS34 3.4 0.8 1.0
C A:CYS36 3.6 0.9 1.0
CA A:CYS36 3.7 0.8 1.0
CA A:CYS37 3.8 1.2 1.0
N A:CYS36 3.9 0.7 1.0
CD A:CD106 4.1 1.4 1.0
O A:CYS50 4.3 1.5 1.0
CD A:CD105 4.3 1.2 1.0
O A:CYS36 4.4 1.2 1.0
CD A:CD101 4.4 1.0 1.0
HA A:CYS37 4.5 1.5 1.0
SG A:CYS44 4.6 1.4 1.0
CA A:CYS50 4.6 1.0 1.0
H A:SER35 4.7 1.7 1.0
CA A:CYS34 4.7 1.0 1.0
C A:CYS50 4.7 1.0 1.0
CB A:CYS57 4.8 1.1 1.0
C A:CYS37 4.8 1.4 1.0
HA A:CYS36 4.8 1.0 1.0
SG A:CYS57 4.9 2.8 1.0
N A:SER35 4.9 0.8 1.0

Reference:

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
Page generated: Fri Aug 28 12:13:14 2020
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