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Zinc in PDB 2cei: Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn

Enzymatic activity of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn

All present enzymatic activity of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn:
1.16.3.1;

Protein crystallography data

The structure of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn, PDB code: 2cei was solved by L.Toussaint, R.R.Crichton, J.P.Declercq, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 103.70 / 1.80
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 179.419, 179.419, 179.419, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 19.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn (pdb code 2cei). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn, PDB code: 2cei:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 2cei

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Zinc binding site 1 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn210

b:29.4
occ:0.50
O A:HOH2136 1.7 31.8 0.5
OE1 A:GLN86 2.1 31.0 1.0
CD A:GLN86 3.1 27.9 1.0
NE2 A:GLN86 3.5 28.8 1.0
O A:HOH2083 4.2 33.3 1.0
CG A:GLN86 4.5 25.9 1.0
CA A:GLN86 4.9 23.1 1.0
CB A:GLN86 5.0 24.1 1.0
N A:LYS87 5.0 24.0 1.0

Zinc binding site 2 out of 8 in 2cei

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Zinc binding site 2 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn211

b:37.4
occ:0.33
O A:HOH2137 2.2 29.8 1.0
OD1 A:ASP131 3.5 31.7 1.0
OG1 A:THR135 3.9 30.3 1.0
OE1 A:GLU134 4.2 28.6 1.0
CG A:ASP131 4.7 30.5 1.0

Zinc binding site 3 out of 8 in 2cei

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Zinc binding site 3 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn212

b:25.6
occ:1.00
OE1 A:GLU27 2.1 23.0 1.0
OE1 A:GLU62 2.1 24.2 1.0
ND1 A:HIS65 2.3 27.0 1.0
O A:HOH2138 2.3 26.5 1.0
CD A:GLU27 3.0 23.7 1.0
CD A:GLU62 3.1 24.7 1.0
CE1 A:HIS65 3.2 31.5 1.0
ZN A:ZN213 3.3 27.4 1.0
OE2 A:GLU27 3.3 26.7 1.0
CG A:HIS65 3.4 27.0 1.0
OE2 A:GLU62 3.5 27.2 1.0
CB A:HIS65 3.7 22.2 1.0
OE1 A:GLN141 4.0 32.4 1.0
NE2 A:HIS65 4.3 31.6 1.0
CG A:GLU27 4.4 19.6 1.0
CG1 A:VAL110 4.4 22.7 1.0
CD2 A:HIS65 4.5 30.2 1.0
CG A:GLU62 4.5 22.3 1.0
CA A:GLU62 4.6 20.4 1.0
CB A:GLU27 4.8 19.4 1.0
CB A:GLU62 4.8 20.0 1.0
OE1 A:GLU107 5.0 23.5 1.0

Zinc binding site 4 out of 8 in 2cei

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Zinc binding site 4 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn213

b:27.4
occ:1.00
OE2 A:GLU62 2.0 27.2 1.0
OE2 A:GLU107 2.2 29.7 1.0
OE1 A:GLU107 2.3 23.5 1.0
CD A:GLU107 2.6 24.8 1.0
CD A:GLU62 2.9 24.7 1.0
OE1 A:GLU62 3.2 24.2 1.0
ZN A:ZN212 3.3 25.6 1.0
OE1 A:GLN141 3.8 32.4 1.0
CG A:GLU107 4.1 20.9 1.0
O A:HOH2058 4.1 41.7 1.0
CG A:GLU62 4.3 22.3 1.0
NE2 A:GLN141 4.4 26.4 1.0
CE2 A:TYR34 4.5 20.2 1.0
CE1 A:HIS65 4.5 31.5 1.0
CD A:GLN141 4.5 29.4 1.0
ND1 A:HIS65 4.6 27.0 1.0
OH A:TYR34 4.7 25.4 1.0
O A:HOH2138 4.7 26.5 1.0
CB A:GLU107 5.0 20.9 1.0

Zinc binding site 5 out of 8 in 2cei

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Zinc binding site 5 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn214

b:35.6
occ:0.25
NE2 A:HIS173 2.2 32.6 1.0
O A:HOH2139 2.3 13.4 0.2
CE1 A:HIS173 2.9 33.0 1.0
CD2 A:HIS173 3.4 30.5 1.0
ND1 A:HIS173 4.2 32.1 1.0
CG A:HIS173 4.4 27.7 1.0

Zinc binding site 6 out of 8 in 2cei

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Zinc binding site 6 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn215

b:29.2
occ:1.00
O A:HOH2140 2.1 36.0 1.0
NE2 A:HIS60 2.1 32.2 1.0
CE1 A:HIS60 2.4 34.0 1.0
CD2 A:HIS60 3.5 34.1 1.0
ND1 A:HIS60 3.7 34.8 1.0
CG A:HIS60 4.2 27.7 1.0
CD2 A:LEU56 4.4 22.1 1.0
CD1 A:LEU56 4.6 18.1 1.0
CG A:LEU56 4.6 22.1 1.0

Zinc binding site 7 out of 8 in 2cei

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Zinc binding site 7 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn216

b:32.2
occ:1.00
NE2 A:HIS118 2.0 26.0 1.0
O A:HOH2141 2.2 28.9 1.0
SG A:CYS130 2.3 25.1 1.0
CE1 A:HIS118 2.9 27.6 1.0
CD2 A:HIS118 3.0 26.7 1.0
OE2 A:GLU134 3.0 28.3 1.0
CB A:CYS130 3.3 23.0 1.0
ZN A:ZN220 3.3 31.9 1.0
CD A:GLU134 4.0 27.1 1.0
OG1 A:THR122 4.0 28.7 1.0
ND1 A:HIS118 4.0 26.5 1.0
CG A:HIS118 4.1 24.8 1.0
O A:HOH2068 4.1 27.6 1.0
CA A:CYS130 4.3 22.7 1.0
OE1 A:GLU134 4.7 28.6 1.0
CG A:GLU134 4.8 26.9 1.0
C A:CYS130 4.8 23.5 1.0
O A:HOH2042 4.9 50.8 1.0
O A:CYS130 5.0 23.6 1.0

Zinc binding site 8 out of 8 in 2cei

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Zinc binding site 8 out of 8 in the Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Recombinant Human H Ferritin, K86Q Mutant, Soaked with Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn220

b:31.9
occ:1.00
OE2 A:GLU134 1.9 28.3 1.0
CD A:GLU134 2.7 27.1 1.0
OE1 A:GLU134 2.8 28.6 1.0
ZN A:ZN216 3.3 32.2 1.0
SG A:CYS130 3.7 25.1 1.0
CG A:GLU134 4.2 26.9 1.0
NE2 A:HIS118 4.5 26.0 1.0

Reference:

L.Toussaint, L.Bertrand, L.Hue, R.R.Crichton, J.P.Declercq. High-Resolution X-Ray Structures of Human Apoferritin H-Chain Mutants Correlated with Their Activity and Metal-Binding Sites. J.Mol.Biol. V. 365 440 2007.
ISSN: ISSN 0022-2836
PubMed: 17070541
DOI: 10.1016/J.JMB.2006.10.010
Page generated: Wed Dec 16 03:19:11 2020

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