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Copper in PDB 4dyy: Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1

Enzymatic activity of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1

All present enzymatic activity of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1:
1.16.3.1;

Protein crystallography data

The structure of Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1, PDB code: 4dyy 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) 89.80 / 1.90
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 179.594, 179.594, 179.594, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 24.1

Other elements in 4dyy:

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

Calcium (Ca) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1 (pdb code 4dyy). 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, PDB code: 4dyy:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 4dyy

Go back to Copper Binding Sites List in 4dyy
Copper binding site 1 out of 3 in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:37.5
occ:1.00
OE1 A:GLU62 1.9 28.8 1.0
OE1 A:GLU27 2.0 26.9 1.0
ND1 A:HIS65 2.1 26.4 1.0
O A:HOH315 2.4 40.9 1.0
CD A:GLU62 2.8 27.4 1.0
CG A:HIS65 3.0 25.5 1.0
CD A:GLU27 3.0 25.0 1.0
CE1 A:HIS65 3.2 27.7 1.0
CB A:HIS65 3.2 23.9 1.0
OE2 A:GLU62 3.2 28.9 1.0
OE2 A:GLU27 3.5 24.9 1.0
CA A:GLU62 4.0 24.3 1.0
OE1 A:GLN141 4.1 31.2 1.0
CG A:GLU62 4.1 25.6 1.0
CD2 A:HIS65 4.2 26.1 1.0
CB A:GLU62 4.2 24.3 1.0
NE2 A:HIS65 4.2 26.3 1.0
CG A:GLU27 4.3 23.7 1.0
O A:HOH403 4.3 43.5 1.0
O A:GLU62 4.6 24.2 1.0
CB A:GLU27 4.6 23.5 1.0
CG1 A:VAL110 4.7 26.0 1.0
CA A:HIS65 4.7 23.8 1.0
C A:GLU62 4.8 24.1 1.0
CA A:GLU27 4.9 23.2 1.0
N A:GLU62 5.0 24.1 1.0

Copper binding site 2 out of 3 in 4dyy

Go back to Copper Binding Sites List in 4dyy
Copper binding site 2 out of 3 in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:28.4
occ:1.00
NE2 A:HIS60 2.1 25.9 1.0
NE2 A:HIS56 2.5 28.9 1.0
O A:HOH404 2.9 42.7 1.0
CE1 A:HIS60 3.1 26.1 1.0
CD2 A:HIS60 3.1 24.9 1.0
CD2 A:HIS56 3.2 26.8 1.0
CE1 A:HIS56 3.7 27.8 1.0
O2 A:EDO206 4.0 31.4 1.0
ND1 A:HIS60 4.2 26.2 1.0
CG A:HIS60 4.2 24.2 1.0
CG A:HIS56 4.4 24.8 1.0
C1 A:EDO206 4.6 31.6 1.0
ND1 A:HIS56 4.6 27.5 1.0
CD1 A:LEU35 4.7 24.5 1.0
C2 A:EDO206 4.9 33.2 1.0

Copper binding site 3 out of 3 in 4dyy

Go back to Copper Binding Sites List in 4dyy
Copper binding site 3 out of 3 in the Crystal Structure of the Cu-Adduct of Human H-Ferritin Variant MIC1


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu203

b:36.3
occ:0.25
NE2 A:HIS173 2.2 30.1 1.0
O A:HOH386 2.8 29.8 0.2
O A:HOH421 2.9 26.9 0.2
CE1 A:HIS173 3.0 30.2 1.0
CD2 A:HIS173 3.3 28.1 1.0
ND1 A:HIS173 4.2 29.9 1.0
CG A:HIS173 4.4 27.3 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: Wed Jul 31 02:44:15 2024

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