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Chlorine in PDB 9eq9: Iron Loaded Mitochondrial Ferritin, Anaerobic

Enzymatic activity of Iron Loaded Mitochondrial Ferritin, Anaerobic

All present enzymatic activity of Iron Loaded Mitochondrial Ferritin, Anaerobic:
1.16.3.1;

Protein crystallography data

The structure of Iron Loaded Mitochondrial Ferritin, Anaerobic, PDB code: 9eq9 was solved by Z.Bugg, J.M.Bradley, N.E.Le Brun, A.M.Hemmings, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.22 / 1.84
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 177.43, 177.43, 177.43, 90, 90, 90
R / Rfree (%) 20.4 / 24.7

Other elements in 9eq9:

The structure of Iron Loaded Mitochondrial Ferritin, Anaerobic also contains other interesting chemical elements:

Magnesium (Mg) 10 atoms
Iron (Fe) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Iron Loaded Mitochondrial Ferritin, Anaerobic (pdb code 9eq9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 8 binding sites of Chlorine where determined in the Iron Loaded Mitochondrial Ferritin, Anaerobic, PDB code: 9eq9:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Chlorine binding site 1 out of 8 in 9eq9

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Chlorine binding site 1 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl215

b:50.9
occ:0.25
 FE A:FE204 2.2 91.3 0.2
HD2 A:HIS173 3.8 45.9 1.0
NE2 A:HIS173 3.8 34.8 1.0
CD2 A:HIS173 4.2 38.1 1.0
CL A:CL216 4.4 67.8 0.2
CE1 A:HIS173 5.0 40.5 1.0

Chlorine binding site 2 out of 8 in 9eq9

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Chlorine binding site 2 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl216

b:67.8
occ:0.25
 FE A:FE204 2.2 91.3 0.2
HE1 A:HIS173 2.5 48.8 1.0
NE2 A:HIS173 2.8 34.8 1.0
CE1 A:HIS173 2.9 40.5 1.0
HD22 A:LEU169 3.7 47.9 1.0
CD2 A:HIS173 4.1 38.1 1.0
ND1 A:HIS173 4.2 33.0 1.0
HD21 A:LEU169 4.4 47.9 1.0
CD2 A:LEU169 4.4 39.8 1.0
CL A:CL215 4.4 50.9 0.2
HD23 A:LEU169 4.5 47.9 1.0
HD2 A:HIS173 4.7 45.9 1.0
HD1 A:HIS173 4.8 39.8 1.0
CG A:HIS173 4.8 31.3 1.0

Chlorine binding site 3 out of 8 in 9eq9

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Chlorine binding site 3 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl217

b:38.4
occ:0.80
 H A:ASP84 2.4 36.0 1.0
HA A:GLN83 2.8 34.1 1.0
O A:HOH362 3.0 31.7 1.0
HB3 A:GLN83 3.0 43.0 1.0
N A:ASP84 3.2 29.9 1.0
CA A:GLN83 3.5 28.3 1.0
HG2 A:GLN83 3.5 48.1 1.0
CB A:GLN83 3.6 35.7 1.0
CG A:ASP84 3.7 33.5 1.0
OD2 A:ASP84 3.7 39.6 1.0
C A:GLN83 3.8 27.0 1.0
OD1 A:ASP84 3.9 32.7 1.0
CG A:GLN83 4.1 39.9 1.0
HB2 A:ASP84 4.1 35.0 1.0
CA A:ASP84 4.3 27.1 1.0
CB A:ASP84 4.3 29.9 1.0
O A:HOH348 4.3 42.6 1.0
MG A:MG207 4.4 30.3 0.5
HB2 A:GLN83 4.5 43.0 1.0
HG3 A:GLN83 4.5 48.1 1.0
O A:LEU82 4.7 34.4 1.0
HA A:ASP84 4.7 31.7 1.0
N A:GLN83 4.8 41.1 1.0

Chlorine binding site 4 out of 8 in 9eq9

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Chlorine binding site 4 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl218

b:63.7
occ:0.82
 HG A:SER95 2.7 42.3 1.0
HB2 A:HIS98 2.8 41.7 1.0
HG3 A:PRO161 2.9 64.8 1.0
OG A:SER95 3.0 35.1 1.0
HB3 A:SER95 3.1 45.2 1.0
HB3 A:GLU94 3.5 55.9 1.0
CB A:SER95 3.5 37.5 1.0
CB A:HIS98 3.8 34.6 1.0
CG A:PRO161 3.8 53.9 1.0
HB3 A:HIS98 3.9 41.7 1.0
HB3 A:PRO161 4.0 71.8 1.0
H A:HIS98 4.0 41.2 1.0
HB2 A:GLU94 4.1 55.9 1.0
HB2 A:SER95 4.1 45.2 1.0
CB A:GLU94 4.2 46.4 1.0
HG2 A:PRO161 4.3 64.8 1.0
CB A:PRO161 4.4 59.7 1.0
CL A:CL219 4.4 65.5 1.0
CG A:HIS98 4.5 36.8 1.0
HD3 A:PRO161 4.5 79.2 1.0
N A:SER95 4.5 43.1 1.0
C A:GLU94 4.5 47.8 1.0
HB2 A:PRO161 4.6 71.8 1.0
OE2 A:GLU94 4.6 76.9 1.0
N A:HIS98 4.6 34.2 1.0
O A:GLU94 4.6 42.1 1.0
CA A:SER95 4.6 33.3 1.0
HD1 A:HIS98 4.7 51.4 1.0
HB3 A:LEU97 4.7 45.1 1.0
CA A:HIS98 4.7 29.2 1.0
H A:SER95 4.8 51.9 1.0
CD A:PRO161 4.8 65.8 1.0
ND1 A:HIS98 4.8 42.7 1.0
HA A:HIS98 4.9 35.2 1.0

Chlorine binding site 5 out of 8 in 9eq9

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Chlorine binding site 5 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl219

b:65.5
occ:1.00
 HD1 A:HIS98 1.7 51.4 1.0
ND1 A:HIS98 2.4 42.7 1.0
OE1 A:GLU101 3.3 63.8 1.0
CE1 A:HIS98 3.3 45.0 1.0
HE1 A:HIS98 3.4 54.1 1.0
HB2 A:HIS98 3.4 41.7 1.0
CG A:HIS98 3.5 36.8 1.0
HA A:HIS98 3.6 35.2 1.0
CB A:HIS98 3.8 34.6 1.0
CA A:HIS98 4.2 29.2 1.0
CL A:CL218 4.4 63.7 0.8
NE2 A:HIS98 4.4 48.3 1.0
CD A:GLU101 4.5 50.6 1.0
CD2 A:HIS98 4.5 39.8 1.0
HB2 A:GLU101 4.7 38.9 1.0
HB3 A:HIS98 4.7 41.7 1.0

Chlorine binding site 6 out of 8 in 9eq9

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Chlorine binding site 6 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl220

b:56.2
occ:0.99
 HD22 A:ASN74 2.6 49.2 1.0
HA A:ARG71 2.9 36.1 1.0
HG3 A:ARG71 3.0 60.2 1.0
HB2 A:ASN74 3.3 38.8 1.0
HB2 A:ARG71 3.4 43.4 1.0
ND2 A:ASN74 3.5 40.9 1.0
HB3 A:ASN74 3.6 38.8 1.0
CA A:ARG71 3.7 29.9 1.0
CG A:ARG71 3.8 50.0 1.0
CB A:ARG71 3.8 36.0 1.0
CB A:ASN74 3.8 32.2 1.0
HD21 A:ASN74 4.1 49.2 1.0
HD2 A:ARG71 4.1 59.3 1.0
CG A:ASN74 4.2 36.3 1.0
O A:ARG71 4.4 38.4 1.0
HG2 A:ARG71 4.5 60.2 1.0
CD A:ARG71 4.5 49.3 1.0
C A:ARG71 4.6 34.4 1.0
N A:ARG71 4.7 27.1 1.0
HB3 A:ARG71 4.8 43.4 1.0
HG3 A:GLN75 4.8 59.0 1.0
O A:MET70 4.9 40.8 1.0

Chlorine binding site 7 out of 8 in 9eq9

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Chlorine binding site 7 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl221

b:47.7
occ:0.59
 H A:ASP91 2.3 54.8 1.0
H A:ASP92 2.4 55.3 1.0
HA A:GLN90 3.0 44.9 1.0
HB3 A:GLN90 3.1 49.8 1.0
N A:ASP91 3.1 45.5 1.0
N A:ASP92 3.3 45.9 1.0
HB3 A:ASP92 3.3 72.6 1.0
CA A:GLN90 3.7 37.3 1.0
CB A:GLN90 3.8 41.4 1.0
C A:GLN90 3.9 51.9 1.0
O A:ASP92 3.9 44.2 1.0
HB2 A:ASP91 3.9 70.2 1.0
CA A:ASP91 4.0 62.8 1.0
CB A:ASP92 4.1 60.4 1.0
CA A:ASP92 4.1 62.9 1.0
C A:ASP91 4.1 46.9 1.0
HB2 A:ASP92 4.4 72.6 1.0
C A:ASP92 4.4 34.6 1.0
HB2 A:GLN90 4.5 49.8 1.0
CB A:ASP91 4.5 58.3 1.0
HG2 A:GLN90 4.5 53.7 1.0
CG A:GLN90 4.8 44.6 1.0
HA A:ASP91 4.9 75.5 1.0
O A:GLU89 4.9 59.4 1.0
O A:HOH317 4.9 64.5 1.0
OE1 A:GLN90 5.0 61.4 1.0
N A:GLN90 5.0 38.2 1.0
HA A:ASP92 5.0 75.6 1.0

Chlorine binding site 8 out of 8 in 9eq9

Go back to Chlorine Binding Sites List in 9eq9
Chlorine binding site 8 out of 8 in the Iron Loaded Mitochondrial Ferritin, Anaerobic


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Iron Loaded Mitochondrial Ferritin, Anaerobic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl222

b:101.1
occ:1.00
 HG3 A:GLU167 2.5 55.3 1.0
H A:GLU167 2.5 34.7 1.0
O A:ALA163 2.6 60.7 1.0
HB2 A:GLU167 2.9 41.8 1.0
O A:PRO161 3.0 85.5 1.0
CG A:GLU167 3.3 45.9 1.0
HB3 A:ALA166 3.3 45.8 1.0
N A:GLU167 3.4 28.8 1.0
HA A:PRO161 3.4 74.6 1.0
CB A:GLU167 3.5 34.7 1.0
C A:PRO161 3.6 59.8 1.0
H A:ALA166 3.6 48.1 1.0
HA A:ALA160 3.8 52.6 1.0
C A:ALA163 3.8 66.8 1.0
CD A:GLU167 3.8 53.3 1.0
OE1 A:GLU167 3.9 68.8 1.0
HA2 A:GLY164 4.0 62.0 1.0
CA A:PRO161 4.0 62.0 1.0
N A:ALA166 4.0 40.0 1.0
HG2 A:GLU167 4.0 55.3 1.0
CA A:GLU167 4.1 34.7 1.0
O A:GLY164 4.2 49.9 1.0
C A:GLY164 4.2 38.5 1.0
CB A:ALA166 4.2 38.0 1.0
H A:TYR168 4.3 44.1 1.0
HB3 A:GLU167 4.3 41.8 1.0
C A:ALA166 4.4 28.7 1.0
HB2 A:ALA160 4.4 45.0 1.0
CA A:GLY164 4.4 51.5 1.0
CA A:ALA166 4.4 35.3 1.0
HB1 A:ALA160 4.5 45.0 1.0
N A:GLY164 4.6 62.5 1.0
OE2 A:GLU167 4.6 56.5 1.0
CA A:ALA160 4.6 43.7 1.0
N A:ASP162 4.6 48.8 1.0
N A:LEU165 4.7 41.5 1.0
N A:ALA163 4.7 43.1 1.0
HB2 A:ALA166 4.7 45.8 1.0
H A:ALA163 4.7 52.0 1.0
HB2 A:PRO161 4.7 71.8 1.0
CB A:ALA160 4.7 37.4 1.0
HB3 A:ALA163 4.7 63.8 1.0
HA A:GLU167 4.7 41.8 1.0
C A:LEU165 4.8 33.6 1.0
CA A:ALA163 4.8 42.8 1.0
HB1 A:ALA166 4.8 45.8 1.0
CB A:PRO161 4.9 59.7 1.0
N A:TYR168 4.9 36.6 1.0
H A:LEU165 5.0 49.9 1.0
C A:ASP162 5.0 47.6 1.0

Reference:

J.M.Bradley, Z.Bugg, G.R.Moore, A.M.Hemmings, N.Le-Brun. The Core Nucleation Site of Human Mitochondrial Ferritin: Observation of the Nascent Mineral To Be Published.
Page generated: Sun Jul 13 16:32:43 2025

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