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Iron in PDB 28kb: Iron Loaded Human H-Chain Ferritin, 3 Hour Oxygen Soak

Enzymatic activity of Iron Loaded Human H-Chain Ferritin, 3 Hour Oxygen Soak

All present enzymatic activity of Iron Loaded Human H-Chain Ferritin, 3 Hour Oxygen Soak:
1.16.3.1;

Protein crystallography data

The structure of Iron Loaded Human H-Chain Ferritin, 3 Hour Oxygen Soak, PDB code: 28kb 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) 53.16 / 1.83
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 184.16, 184.16, 184.16, 90, 90, 90
R / Rfree (%) 19.2 / 22.8

Other elements in 28kb:

The structure of Iron Loaded Human H-Chain Ferritin, 3 Hour Oxygen Soak also contains other interesting chemical elements:

Magnesium (Mg) 6 atoms
Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Iron Loaded Human H-Chain Ferritin, 3 Hour Oxygen Soak (pdb code 28kb). 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, 3 Hour Oxygen Soak, PDB code: 28kb:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 28kb

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Iron binding site 1 out of 6 in the Iron Loaded Human H-Chain Ferritin, 3 Hour 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, 3 Hour Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:24.9
occ:0.25
 O A:HOH396 2.2 25.5 0.2
NE2 A:HIS173 2.2 26.5 1.0
CL A:CL213 2.4 26.2 0.2
CE1 A:HIS173 3.1 29.9 1.0
CD2 A:HIS173 3.3 27.0 1.0
ND1 A:HIS173 4.3 28.1 1.0
CG A:HIS173 4.4 24.6 1.0
O A:HOH424 4.6 42.9 1.0

Iron binding site 2 out of 6 in 28kb

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Iron binding site 2 out of 6 in the Iron Loaded Human H-Chain Ferritin, 3 Hour 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, 3 Hour Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:33.6
occ:0.90
 OE2 A:GLU62 2.0 34.0 1.0
O A:HOH344 2.1 33.2 1.0
OE1 A:GLU107 2.2 33.4 1.0
OE2 A:GLU107 2.2 36.8 1.0
O A:HOH382 2.4 24.7 1.0
O A:HOH395 2.4 38.0 1.0
CD A:GLU107 2.5 35.8 1.0
CD A:GLU62 3.0 31.5 1.0
OE1 A:GLU62 3.3 32.4 1.0
FE A:FE204 3.3 30.7 1.0
OE1 A:GLN141 3.9 36.7 1.0
CG A:GLU107 4.1 30.0 1.0
NE2 A:GLN141 4.1 35.7 1.0
O A:HOH423 4.1 45.8 1.0
CG A:GLU62 4.3 27.4 1.0
O A:HOH364 4.3 38.0 1.0
CD A:GLN141 4.3 36.7 1.0
O A:HOH324 4.4 29.3 1.0
O A:HOH318 4.5 52.9 1.0
OH A:TYR34 4.6 36.0 1.0
CE2 A:TYR34 4.6 28.0 1.0
ND1 A:HIS65 4.7 30.9 0.5
CE1 A:HIS65 4.7 36.4 0.5
CB A:GLU107 4.8 29.1 1.0

Iron binding site 3 out of 6 in 28kb

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Iron binding site 3 out of 6 in the Iron Loaded Human H-Chain Ferritin, 3 Hour 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, 3 Hour Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe203

b:47.0
occ:0.20
 O A:HOH309 1.9 61.2 1.0
O A:HOH321 2.1 61.6 1.0
OE2 A:GLU61 2.1 50.8 0.6
NE2 A:HIS57 2.4 49.1 1.0
OE1 A:GLU61 2.8 52.9 0.4
CD A:GLU61 3.0 45.0 0.4
CD A:GLU61 3.2 44.2 0.6
CE1 A:HIS57 3.3 52.3 1.0
O A:HOH303 3.3 60.0 1.0
CD2 A:HIS57 3.4 52.8 1.0
OE2 A:GLU61 3.4 49.7 0.4
CG A:GLU61 3.7 41.5 0.4
CG A:GLU61 3.7 41.9 0.6
O A:HOH342 3.9 53.0 1.0
OE1 A:GLU61 4.2 46.1 0.6
O A:HOH304 4.3 64.3 1.0
ND1 A:HIS57 4.4 53.7 1.0
CG A:HIS57 4.5 44.6 1.0
FE A:FE206 4.6 56.6 0.3
O A:HOH372 4.8 56.5 1.0

Iron binding site 4 out of 6 in 28kb

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Iron binding site 4 out of 6 in the Iron Loaded Human H-Chain Ferritin, 3 Hour 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, 3 Hour Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe204

b:30.7
occ:1.00
 OE1 A:GLU27 2.1 28.4 1.0
OE1 A:GLU62 2.1 32.4 1.0
O A:HOH324 2.2 29.3 1.0
O A:HOH344 2.2 33.2 1.0
ND1 A:HIS65 2.3 30.9 0.5
ND1 A:HIS65 2.5 30.7 0.5
O A:HOH382 2.6 24.7 1.0
CD A:GLU27 3.1 33.3 1.0
CD A:GLU62 3.1 31.5 1.0
CE1 A:HIS65 3.2 36.4 0.5
FE A:FE202 3.3 33.6 0.9
CG A:HIS65 3.4 30.8 0.5
CE1 A:HIS65 3.4 33.2 0.5
OE2 A:GLU62 3.4 34.0 1.0
OE2 A:GLU27 3.4 31.8 1.0
CG A:HIS65 3.5 31.1 0.5
CB A:HIS65 3.7 28.9 0.5
CB A:HIS65 3.8 29.0 0.5
OE1 A:GLN141 4.1 36.7 1.0
NE2 A:HIS65 4.4 41.7 0.5
CG A:GLU27 4.5 24.8 1.0
CD2 A:HIS65 4.5 30.6 0.5
CG A:GLU62 4.5 27.4 1.0
NE2 A:HIS65 4.6 34.0 0.5
CD2 A:HIS65 4.6 32.5 0.5
CA A:GLU62 4.7 26.0 1.0
CG1 A:VAL110 4.7 32.7 1.0
CB A:GLU27 4.8 26.4 1.0
CB A:GLU62 4.8 26.0 1.0
O A:HOH395 4.9 38.0 1.0
CD A:GLN141 5.0 36.7 1.0
OE1 A:GLU107 5.0 33.4 1.0

Iron binding site 5 out of 6 in 28kb

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Iron binding site 5 out of 6 in the Iron Loaded Human H-Chain Ferritin, 3 Hour 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, 3 Hour Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe205

b:43.2
occ:0.30
 O A:HOH342 2.0 53.0 1.0
O A:HOH372 2.0 56.5 1.0
OE1 A:GLU61 2.1 46.1 0.6
O A:HOH410 2.1 51.1 1.0
O A:HOH318 2.3 52.9 1.0
OE1 A:GLN58 2.3 40.8 1.0
CD A:GLU61 3.0 44.2 0.6
OE2 A:GLU61 3.3 50.8 0.6
CD A:GLN58 3.3 43.8 1.0
NE2 A:GLN58 3.7 42.6 1.0
O A:HOH309 4.2 61.2 1.0
O A:HOH340 4.3 48.7 1.0
O A:HOH366 4.3 51.2 1.0
O A:HOH423 4.3 45.8 1.0
CG A:GLU61 4.4 41.9 0.6
O A:HOH364 4.4 38.0 1.0
O A:HOH395 4.6 38.0 1.0
CG A:GLN58 4.7 32.7 1.0
CG A:GLU61 4.7 41.5 0.4
CB A:GLU61 4.8 34.9 0.6
OE2 A:GLU147 4.9 42.8 1.0
CB A:GLU61 4.9 35.5 0.4
O A:HOH312 5.0 57.1 1.0

Iron binding site 6 out of 6 in 28kb

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Iron binding site 6 out of 6 in the Iron Loaded Human H-Chain Ferritin, 3 Hour 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, 3 Hour Oxygen Soak within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe206

b:56.6
occ:0.30
 O A:HOH304 2.1 64.3 1.0
O A:HOH303 2.5 60.0 1.0
OE1 A:GLU64 2.6 69.5 1.0
OE2 A:GLU61 2.7 49.7 0.4
OE1 A:GLU61 2.8 52.9 0.4
CD A:GLU61 3.1 45.0 0.4
O A:HOH321 3.5 61.6 1.0
CD A:GLU64 3.6 67.9 1.0
OE2 A:GLU64 4.1 80.4 1.0
O A:HOH306 4.2 57.0 1.0
O A:HOH312 4.4 57.1 1.0
CG A:GLU61 4.5 41.5 0.4
CG A:GLU61 4.6 41.9 0.6
FE A:FE203 4.6 47.0 0.2
CG A:GLU64 4.9 45.2 1.0
CB A:GLU64 4.9 32.9 1.0
OE2 A:GLU61 4.9 50.8 0.6
CB A:GLU61 5.0 35.5 0.4

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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