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Copper in PDB 4dz0: Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore

Enzymatic activity of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore

All present enzymatic activity of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore:
1.16.3.1;

Protein crystallography data

The structure of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore, PDB code: 4dz0 was solved by F.A.Tezcan, D.J.E.Huard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.84 / 2.50
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 180.434, 180.434, 180.434, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 30

Other elements in 4dz0:

The structure of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore (pdb code 4dz0). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore, PDB code: 4dz0:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 4dz0

Go back to Copper Binding Sites List in 4dz0
Copper binding site 1 out of 3 in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:41.5
occ:1.00
NE2 A:HIS60 2.1 32.5 1.0
NE2 A:HIS56 2.5 36.5 1.0
CE1 A:HIS60 2.9 32.5 1.0
CD2 A:HIS60 3.1 32.4 1.0
CD2 A:HIS56 3.2 36.0 1.0
CE1 A:HIS56 3.7 35.9 1.0
ND1 A:HIS60 4.1 33.0 1.0
CG A:HIS60 4.2 32.9 1.0
CG A:HIS56 4.5 34.4 1.0
ND1 A:HIS56 4.7 35.3 1.0
CD1 A:LEU35 4.7 34.2 1.0

Copper binding site 2 out of 3 in 4dz0

Go back to Copper Binding Sites List in 4dz0
Copper binding site 2 out of 3 in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu203

b:55.1
occ:1.00
OE1 A:GLU62 2.0 36.2 1.0
OE1 A:GLU27 2.1 35.7 1.0
ND1 A:HIS65 2.2 35.8 1.0
CD A:GLU62 2.9 35.6 1.0
CG A:HIS65 3.1 34.9 1.0
CD A:GLU27 3.1 33.8 1.0
CB A:HIS65 3.2 34.1 1.0
CE1 A:HIS65 3.2 35.5 1.0
OE2 A:GLU62 3.4 37.0 1.0
OE2 A:GLU27 3.6 32.7 1.0
CA A:GLU62 4.1 33.8 1.0
CG A:GLU62 4.2 34.1 1.0
CD2 A:HIS65 4.2 35.7 1.0
OE1 A:GLN141 4.2 36.5 1.0
O A:HOH319 4.2 55.4 1.0
CG A:GLU27 4.3 32.2 1.0
NE2 A:HIS65 4.3 36.3 1.0
CB A:GLU62 4.3 34.0 1.0
CG1 A:VAL110 4.5 37.4 1.0
CB A:GLU27 4.6 31.7 1.0
O A:GLU62 4.6 33.9 1.0
CA A:HIS65 4.8 33.9 1.0
C A:GLU62 4.9 33.9 1.0
CA A:GLU27 4.9 31.7 1.0

Copper binding site 3 out of 3 in 4dz0

Go back to Copper Binding Sites List in 4dz0
Copper binding site 3 out of 3 in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 Labeled with A Dansyl Fluorophore within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu204

b:70.6
occ:0.25
NE2 A:HIS173 2.4 35.3 1.0
CE1 A:HIS173 2.9 34.9 1.0
CD2 A:HIS173 3.7 34.7 1.0
ND1 A:HIS173 4.2 35.3 1.0
CG A:HIS173 4.6 34.5 1.0

Reference:

D.J.Huard, K.M.Kane, F.A.Tezcan. Re-Engineering Protein Interfaces Yields Copper-Inducible Ferritin Cage Assembly. Nat.Chem.Biol. V. 9 169 2013.
ISSN: ISSN 1552-4450
PubMed: 23340339
DOI: 10.1038/NCHEMBIO.1163
Page generated: Sun Dec 13 11:13:59 2020

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