Chlorine in PDB 3ka6: Frog M-Ferritin, Eed Mutant, with Cobalt

All present enzymatic activity of Frog M-Ferritin, Eed Mutant, with Cobalt:
1.16.3.1;

The structure of Frog M-Ferritin, Eed Mutant, with Cobalt, PDB code: 3ka6 was solved by T.Tosha, H.L.Ng, E.Theil, T.Alber, O.Bhattasali, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.40
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	183.708, 183.708, 183.708, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16.6

The structure of Frog M-Ferritin, Eed Mutant, with Cobalt also contains other interesting chemical elements:

Cobalt	(Co)	10 atoms
Magnesium	(Mg)	5 atoms

The binding sites of Chlorine atom in the Frog M-Ferritin, Eed Mutant, with Cobalt (pdb code 3ka6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Frog M-Ferritin, Eed Mutant, with Cobalt, PDB code: 3ka6:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Frog M-Ferritin, Eed Mutant, with Cobalt


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Frog M-Ferritin, Eed Mutant, with Cobalt within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl189 b:13.4 occ:0.25 CO A:CO176 2.3 13.6 0.2 NE2 A:HIS169 3.2 12.6 1.0 CE1 A:HIS169 3.3 13.8 1.0 CD2 A:LEU165 3.6 13.8 1.0 CD2 A:HIS169 4.4 12.2 1.0 ND1 A:HIS169 4.5 13.1 1.0 O A:HOH430 4.7 16.1 0.2

Chlorine binding site 2 out of 4 in the Frog M-Ferritin, Eed Mutant, with Cobalt


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Frog M-Ferritin, Eed Mutant, with Cobalt within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl190 b:22.2 occ:1.00 O A:HOH511 2.9 35.1 1.0 O A:HOH299 3.1 21.2 1.0 N A:GLU136 3.2 13.7 1.0 C A:GLU132 3.3 13.1 1.0 N A:TYR133 3.4 10.6 1.0 N A:GLU135 3.4 11.5 1.0 CG A:GLU136 3.5 21.6 0.5 O A:SER131 3.5 15.6 1.0 CB A:GLU135 3.6 14.0 1.0 O A:GLU132 3.7 15.3 1.0 C A:TYR133 3.7 10.5 1.0 C A:SER131 3.8 13.8 1.0 CA A:GLU135 3.8 12.2 1.0 CA A:GLU132 3.8 12.9 1.0 N A:GLU132 3.9 13.6 1.0 CA A:TYR133 3.9 11.0 1.0 N A:LEU134 3.9 10.6 1.0 C A:GLU135 3.9 11.9 1.0 CB A:GLU136 3.9 15.3 0.5 CB A:GLU136 3.9 14.3 0.5 O A:GLU130 4.0 15.6 1.0 O A:HOH242 4.0 39.3 1.0 O A:TYR133 4.1 12.0 1.0 CA A:GLU136 4.1 12.9 0.5 CA A:GLU136 4.1 13.4 0.5 O A:HOH303 4.2 42.4 1.0 OE2 A:GLU136 4.3 31.4 0.5 CG A:GLU135 4.4 14.2 1.0 C A:LEU134 4.4 10.6 1.0 CD A:GLU136 4.4 28.1 0.5 O A:HOH334 4.6 25.5 1.0 CA A:SER131 4.7 13.9 1.0 CA A:LEU134 4.8 11.4 1.0 C A:GLU130 4.8 12.1 1.0 MG A:MG191 4.9 18.4 1.0 O A:HOH253 4.9 21.2 1.0

Chlorine binding site 3 out of 4 in the Frog M-Ferritin, Eed Mutant, with Cobalt


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Frog M-Ferritin, Eed Mutant, with Cobalt within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl193 b:20.6 occ:1.00 O A:HOH302 3.0 44.3 1.0 O A:HOH288 3.1 42.0 1.0 N A:TYR8 3.3 10.7 1.0 O A:HOH218 3.3 34.0 1.0 N A:ASN7 3.4 10.8 1.0 O A:TYR8 3.5 11.9 1.0 CG A:ARG5 3.6 14.2 1.0 CD A:ARG5 3.6 17.1 1.0 NE A:ARG5 3.6 14.7 1.0 O A:HOH389 3.8 20.5 1.0 C A:GLN6 3.9 10.8 1.0 CA A:GLN6 4.0 11.0 1.0 N A:GLN6 4.0 11.0 1.0 C A:TYR8 4.1 11.4 1.0 CA A:TYR8 4.1 10.2 1.0 CA A:ASN7 4.1 10.7 1.0 C A:ASN7 4.2 10.7 1.0 C A:ARG5 4.2 12.0 1.0 CB A:TYR8 4.4 10.3 1.0 O A:ARG5 4.4 13.1 1.0 CB A:ARG5 4.5 14.2 1.0 O A:GLN6 4.8 11.1 1.0 CZ A:ARG5 4.9 12.0 1.0 CA A:ARG5 5.0 12.1 1.0

Chlorine binding site 4 out of 4 in the Frog M-Ferritin, Eed Mutant, with Cobalt


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Frog M-Ferritin, Eed Mutant, with Cobalt within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl194 b:29.2 occ:1.00 O A:HOH293 3.1 47.5 1.0 N A:SER10 3.1 11.8 1.0 CB A:SER10 3.7 14.1 1.0 CA A:HIS9 3.8 12.3 0.5 CA A:HIS9 3.8 10.8 0.5 O A:HOH218 3.8 34.0 1.0 CD2 A:HIS9 3.8 9.7 0.5 CG A:HIS9 3.9 9.6 0.5 O A:HOH288 3.9 42.0 1.0 C A:HIS9 3.9 10.7 1.0 CA A:SER10 4.0 12.4 1.0 NE2 A:HIS9 4.0 11.0 0.5 ND1 A:HIS9 4.1 9.4 0.5 CE1 A:HIS9 4.1 4.9 0.5 ND1 A:HIS9 4.3 23.3 0.5 CB A:HIS9 4.3 13.7 0.5 O A:TYR8 4.4 11.9 1.0 CG A:HIS9 4.4 19.0 0.5 CB A:HIS9 4.4 11.1 0.5 O A:HOH263 4.7 38.2 1.0 N A:HIS9 4.9 11.3 1.0 CE1 A:HIS9 5.0 22.4 0.5 NH2 A:ARG5 5.0 14.2 1.0

T.Tosha, H.L.Ng, O.Bhattasali, T.Alber, E.C.Theil. Moving Metal Ions Through Ferritin-Protein Nanocages From Three-Fold Pores to Catalytic Sites. J.Am.Chem.Soc. V. 132 14562 2010.
ISSN: ISSN 0002-7863
PubMed: 20866049
DOI: 10.1021/JA105583D