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 / R_free (%)*	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

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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

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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

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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: Wed Jul 31 02:44:15 2024

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