Cadmium in PDB 6gv7: Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52)

The binding sites of Cadmium atom in the Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52) (pdb code 6gv7). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 4 binding sites of Cadmium where determined in the Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52), PDB code: 6gv7:
Jump to Cadmium binding site number: 1; 2; 3; 4;

Cadmium binding site 1 out of 4 in the Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52)


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd101 b:0.0 occ:1.00 NE2 A:HIS36 2.4 0.0 1.0 SG A:CYS32 2.4 0.0 1.0 SG A:CYS49 2.5 0.0 1.0 SG A:CYS7 2.6 0.0 1.0 HE1 A:HIS36 2.7 0.0 1.0 CE1 A:HIS36 2.9 0.0 1.0 HB2 A:CYS49 3.2 0.0 1.0 HB3 A:CYS10 3.3 0.0 1.0 HA A:CYS32 3.3 0.0 1.0 HB2 A:CYS7 3.4 0.0 1.0 CB A:CYS49 3.5 0.0 1.0 HB2 A:CYS10 3.5 0.0 1.0 CB A:CYS32 3.5 0.0 1.0 CB A:CYS7 3.6 0.0 1.0 HB3 A:CYS32 3.6 0.0 1.0 CD2 A:HIS36 3.6 0.0 1.0 CB A:CYS10 3.9 0.0 1.0 HB3 A:CYS7 3.9 0.0 1.0 CA A:CYS32 4.0 0.0 1.0 HB3 A:CYS42 4.0 0.0 1.0 HD2 A:HIS36 4.1 0.0 1.0 HB3 A:CYS49 4.1 0.0 1.0 ND1 A:HIS36 4.1 0.0 1.0 CD A:CD104 4.2 0.0 1.0 CD A:CD102 4.3 0.0 1.0 O A:CYS49 4.4 0.0 1.0 HB2 A:CYS32 4.5 0.0 1.0 C A:CYS49 4.5 0.0 1.0 CG A:HIS36 4.5 0.0 1.0 SG A:CYS10 4.6 0.0 1.0 H A:CYS10 4.6 0.0 1.0 CA A:CYS49 4.6 0.0 1.0 H A:CYS42 4.7 0.0 1.0 N A:CYS32 4.7 0.0 1.0 HA A:PRO41 4.8 0.0 1.0 HD1 A:HIS36 4.9 0.0 1.0 HA A:GLU50 4.9 0.0 1.0

Cadmium binding site 2 out of 4 in the Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52)


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd102 b:0.0 occ:1.00 SG A:CYS10 2.4 0.0 1.0 HB2 A:CYS10 2.4 0.0 1.0 SG A:CYS42 2.5 0.0 1.0 SG A:CYS49 2.6 0.0 1.0 SG A:CYS47 2.6 0.0 1.0 CB A:CYS10 2.9 0.0 1.0 HB3 A:CYS49 3.4 0.0 1.0 HB3 A:CYS42 3.4 0.0 1.0 H A:CYS49 3.5 0.0 1.0 HB3 A:CYS10 3.6 0.0 1.0 CB A:CYS42 3.7 0.0 1.0 CB A:CYS49 3.7 0.0 1.0 H A:CYS42 3.7 0.0 1.0 HA A:CYS10 3.9 0.0 1.0 CD A:CD104 4.0 0.0 1.0 CA A:CYS10 4.0 0.0 1.0 CD A:CD103 4.1 0.0 1.0 N A:CYS49 4.3 0.0 1.0 CD A:CD101 4.3 0.0 1.0 HB2 A:CYS42 4.4 0.0 1.0 CB A:CYS47 4.4 0.0 1.0 HB2 A:CYS49 4.4 0.0 1.0 HB2 A:HIS44 4.5 0.0 1.0 N A:CYS42 4.5 0.0 1.0 SG A:CYS32 4.6 0.0 1.0 SG A:CYS12 4.6 0.0 1.0 CA A:CYS49 4.6 0.0 1.0 CA A:CYS42 4.7 0.0 1.0 HB2 A:CYS47 4.7 0.0 1.0 C A:CYS10 4.9 0.0 1.0 HB3 A:CYS47 4.9 0.0 1.0 H A:CYS47 5.0 0.0 1.0 HE1 A:HIS36 5.0 0.0 1.0 H A:HIS11 5.0 0.0 1.0

Cadmium binding site 3 out of 4 in the Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52)


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd103 b:0.0 occ:1.00 ND1 A:HIS44 2.4 0.0 1.0 SG A:CYS28 2.4 0.0 1.0 SG A:CYS12 2.6 0.0 1.0 SG A:CYS42 2.6 0.0 1.0 HB2 A:CYS42 2.6 0.0 1.0 HB2 A:HIS44 2.8 0.0 1.0 CG A:HIS44 3.0 0.0 1.0 CE1 A:HIS44 3.1 0.0 1.0 CB A:CYS42 3.1 0.0 1.0 HB2 A:CYS28 3.2 0.0 1.0 CB A:CYS28 3.4 0.0 1.0 CB A:HIS44 3.4 0.0 1.0 HE1 A:HIS44 3.5 0.0 1.0 HB2 A:CYS12 3.5 0.0 1.0 CB A:CYS12 3.6 0.0 1.0 HB3 A:CYS28 3.6 0.0 1.0 HB3 A:CYS42 3.6 0.0 1.0 HB3 A:CYS12 3.7 0.0 1.0 CD A:CD104 3.8 0.0 1.0 CD2 A:HIS44 3.8 0.0 1.0 NE2 A:HIS44 3.9 0.0 1.0 HD2 A:PRO43 4.0 0.0 1.0 SG A:CYS10 4.0 0.0 1.0 HB3 A:HIS44 4.0 0.0 1.0 CD A:CD102 4.1 0.0 1.0 H A:HIS44 4.4 0.0 1.0 N A:HIS44 4.4 0.0 1.0 CA A:CYS42 4.4 0.0 1.0 C A:CYS42 4.5 0.0 1.0 CA A:HIS44 4.5 0.0 1.0 HE2 A:HIS44 4.5 0.0 1.0 N A:PRO43 4.6 0.0 1.0 HD2 A:HIS44 4.7 0.0 1.0 HG2 A:PRO43 4.7 0.0 1.0 CD A:PRO43 4.8 0.0 1.0 CA A:CYS28 4.8 0.0 1.0 C A:PRO43 4.9 0.0 1.0 HB2 A:SER29 4.9 0.0 1.0 HA A:CYS42 5.0 0.0 1.0

Cadmium binding site 4 out of 4 in the Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52)


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of Cadmium(II) Form of A44H Mutant of Shortened Metallothionein From Pseudomonas Fluorescens Q2-87 (Residues 1-52) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd104 b:0.0 occ:1.00 SG A:CYS5 2.5 0.0 1.0 SG A:CYS28 2.6 0.0 1.0 SG A:CYS32 2.6 0.0 1.0 SG A:CYS10 2.6 0.0 1.0 HB3 A:CYS10 3.3 0.0 1.0 H A:CYS28 3.3 0.0 1.0 HB3 A:CYS42 3.4 0.0 1.0 HB2 A:CYS32 3.5 0.0 1.0 CB A:CYS32 3.5 0.0 1.0 HB3 A:CYS7 3.6 0.0 1.0 CB A:CYS10 3.6 0.0 1.0 HB2 A:CYS7 3.6 0.0 1.0 HB3 A:CYS32 3.7 0.0 1.0 HB2 A:CYS12 3.7 0.0 1.0 CB A:CYS5 3.8 0.0 1.0 CD A:CD103 3.8 0.0 1.0 HB2 A:CYS5 3.8 0.0 1.0 HB3 A:CYS28 3.9 0.0 1.0 CB A:CYS28 3.9 0.0 1.0 HB2 A:CYS42 3.9 0.0 1.0 HB3 A:CYS5 4.0 0.0 1.0 CD A:CD102 4.0 0.0 1.0 CB A:CYS42 4.0 0.0 1.0 CB A:CYS7 4.1 0.0 1.0 HB2 A:CYS10 4.2 0.0 1.0 CD A:CD101 4.2 0.0 1.0 N A:CYS28 4.2 0.0 1.0 H A:SER29 4.2 0.0 1.0 HB3 A:TYR27 4.2 0.0 1.0 SG A:CYS42 4.3 0.0 1.0 HD2 A:TYR27 4.5 0.0 1.0 SG A:CYS12 4.5 0.0 1.0 CB A:CYS12 4.6 0.0 1.0 O A:CYS10 4.6 0.0 1.0 H A:CYS7 4.6 0.0 1.0 CA A:CYS28 4.6 0.0 1.0 H A:CYS12 4.7 0.0 1.0 HB2 A:CYS28 4.7 0.0 1.0 C A:CYS10 4.8 0.0 1.0 SG A:CYS49 4.8 0.0 1.0 CA A:CYS10 4.8 0.0 1.0 HA A:TYR27 4.9 0.0 1.0 SG A:CYS7 4.9 0.0 1.0 N A:SER29 4.9 0.0 1.0

J.Habjanic, O.Zerbe, E.Freisinger. A Histidine-Rich Pseudomonas Metallothionein with A Disordered Tail Displays Higher Binding Capacity For Cadmium Than Zinc. Metallomics V. 10 1415 2018.
ISSN: ESSN 1756-591X
PubMed: 30191219
DOI: 10.1039/C8MT00193F