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Iron in PDB 28kc: Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak

Enzymatic activity of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak

All present enzymatic activity of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak:
1.16.3.1;

Protein crystallography data

The structure of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak, PDB code: 28kc 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) 105.62 / 1.94
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 182.94, 182.94, 182.94, 90, 90, 90
R / Rfree (%) 16.8 / 19.2

Other elements in 28kc:

The structure of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak (pdb code 28kc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak, PDB code: 28kc:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 28kc

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Iron binding site 1 out of 6 in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:33.0
occ:0.20
 O A:HOH404 2.1 25.8 0.2
NE2 A:HIS173 2.2 30.5 1.0
CL A:CL207 2.5 28.5 0.2
CE1 A:HIS173 3.1 36.9 1.0
CD2 A:HIS173 3.3 34.8 1.0
ND1 A:HIS173 4.3 33.1 1.0
CG A:HIS173 4.4 32.6 1.0

Iron binding site 2 out of 6 in 28kc

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Iron binding site 2 out of 6 in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:39.9
occ:0.80
 OE1 A:GLU62 2.1 33.1 1.0
OE1 A:GLU27 2.1 33.8 1.0
O A:HOH326 2.2 31.7 1.0
O A:HOH303 2.3 37.4 1.0
ND1 A:HIS65 2.4 41.0 1.0
O A:HOH392 2.7 35.1 1.0
CD A:GLU62 3.0 31.6 1.0
CD A:GLU27 3.1 33.3 1.0
CE1 A:HIS65 3.2 59.7 1.0
FE A:FE203 3.3 42.4 0.6
OE2 A:GLU62 3.3 37.8 1.0
CG A:HIS65 3.4 40.8 1.0
OE2 A:GLU27 3.5 35.6 1.0
OE1 A:GLN141 3.7 45.7 1.0
CB A:HIS65 3.8 27.3 1.0
NE2 A:HIS65 4.4 70.0 1.0
CG A:GLU62 4.4 24.7 1.0
CG1 A:VAL110 4.4 29.0 1.0
CG A:GLU27 4.5 24.8 1.0
CD2 A:HIS65 4.5 41.4 1.0
CA A:GLU62 4.6 26.3 1.0
CD A:GLN141 4.7 34.9 1.0
CB A:GLU62 4.7 26.2 1.0
OE1 A:GLU107 4.9 35.7 1.0
CB A:GLU27 4.9 24.8 1.0
O A:HOH423 4.9 45.0 1.0

Iron binding site 3 out of 6 in 28kc

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Iron binding site 3 out of 6 in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe203

b:42.4
occ:0.60
 OE2 A:GLU62 1.8 37.8 1.0
OE1 A:GLU107 2.1 35.7 1.0
O A:HOH303 2.1 37.4 1.0
OE2 A:GLU107 2.2 45.0 1.0
O A:HOH392 2.4 35.1 1.0
O A:HOH423 2.4 45.0 1.0
CD A:GLU107 2.5 40.2 1.0
CD A:GLU62 2.9 31.6 1.0
OE1 A:GLU62 3.2 33.1 1.0
FE A:FE202 3.3 39.9 0.8
OE1 A:GLN141 3.6 45.7 1.0
CG A:GLU107 4.0 29.1 1.0
O A:HOH381 4.2 52.6 1.0
NE2 A:GLN141 4.2 36.7 1.0
CG A:GLU62 4.2 24.7 1.0
CD A:GLN141 4.3 34.9 1.0
O A:HOH326 4.5 31.7 1.0
CE2 A:TYR34 4.5 25.9 1.0
O A:HOH429 4.5 56.2 1.0
ND1 A:HIS65 4.6 41.0 1.0
CE1 A:HIS65 4.6 59.7 1.0
OH A:TYR34 4.6 41.4 1.0
CB A:GLU107 4.8 28.9 1.0
O A:HOH302 4.9 68.5 1.0

Iron binding site 4 out of 6 in 28kc

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Iron binding site 4 out of 6 in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe204

b:38.5
occ:0.48
 O A:HOH331 2.4 45.6 1.0
O A:HOH435 3.0 56.7 1.0
NE2 A:GLN75 3.1 36.0 1.0
CG A:GLN75 3.7 33.5 1.0
CD A:GLN75 3.9 36.7 1.0
NZ A:LYS71 4.1 60.1 1.0
CE A:LYS71 4.5 53.1 1.0
CB A:GLN75 5.0 23.8 1.0

Iron binding site 5 out of 6 in 28kc

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Iron binding site 5 out of 6 in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe205

b:63.5
occ:0.30
 OE2 A:GLU61 1.9 52.7 0.5
NE2 A:HIS57 2.7 51.7 1.0
OE1 A:GLU61 3.0 65.3 0.5
CD A:GLU61 3.1 48.6 0.5
O A:HOH329 3.2 67.9 1.0
O A:HOH365 3.3 66.4 1.0
FE A:FE206 3.3 58.2 0.3
CD2 A:HIS57 3.6 52.7 1.0
CD A:GLU61 3.6 49.4 0.5
CE1 A:HIS57 3.7 53.6 1.0
CG A:GLU61 4.0 43.5 0.5
OE1 A:GLU61 4.0 51.4 0.5
CG A:GLU61 4.0 42.8 0.5
OE2 A:GLU61 4.4 52.9 0.5
ND1 A:HIS57 4.8 61.5 1.0
CG A:HIS57 4.8 56.2 1.0

Iron binding site 6 out of 6 in 28kc

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Iron binding site 6 out of 6 in the Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Iron Loaded Human H-Chain Ferritin, 2 Minute Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe206

b:58.2
occ:0.30
 O A:HOH365 2.0 66.4 1.0
O A:HOH422 2.3 57.6 1.0
OE1 A:GLU61 2.6 51.4 0.5
OE2 A:GLU61 2.7 52.7 0.5
CD A:GLU61 2.9 48.6 0.5
O A:HOH302 3.0 68.5 1.0
OE1 A:GLN58 3.1 47.1 1.0
FE A:FE205 3.3 63.5 0.3
NE2 A:GLN58 3.4 51.5 1.0
CD A:GLN58 3.6 51.3 1.0
O A:HOH428 3.6 58.9 1.0
CD2 A:HIS57 4.1 52.7 1.0
CG A:GLU61 4.3 43.5 0.5
NE2 A:HIS57 4.3 51.7 1.0
O A:HOH403 4.5 55.7 1.0
O A:HOH429 4.7 56.2 1.0
O A:HOH412 4.8 47.3 1.0
OE2 A:GLU147 4.8 46.4 1.0
CG A:GLU61 4.8 42.8 0.5
OE1 A:GLU61 4.8 65.3 0.5

Reference:

Z.Bugg, J.M.Bradley, A.M.Hemmings, N.E.Le Brun. Ferritin Iron Mineralisation: Route of Fe 3+ Transfer From the Ferroxidase Centre to the Inner Cavity of Human H-Chain Ferritin. Angew.Chem.Int.Ed.Engl. 03843 2026.
ISSN: ESSN 1521-3773
PubMed: 42216818
DOI: 10.1002/ANIE.1203843
Page generated: Sun Oct 4 09:32:40 2026

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