Copper in PDB 4dyz: Crystal Structure of the Apo Form of Human H-Ferritin Variant MIC1

Enzymatic activity of Crystal Structure of the Apo Form of Human H-Ferritin Variant MIC1

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

Protein crystallography data

The structure of Crystal Structure of the Apo Form of Human H-Ferritin Variant MIC1, PDB code: 4dyz 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)*	90.54 / 2.30
*Space group*	F 4 3 2
*Cell size a, b, c (Å), α, β, γ (°)*	181.066, 181.066, 181.066, 90.00, 90.00, 90.00
*R / R_free (%)*	21.9 / 27.2

Other elements in 4dyz:

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

Calcium

(Ca)

4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Apo Form of Human H-Ferritin Variant MIC1 (pdb code 4dyz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of the Apo Form of Human H-Ferritin Variant MIC1, PDB code: 4dyz:

Copper binding site 1 out of 1 in 4dyz

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Copper Binding Sites List in 4dyz

Copper binding site 1 out of 1 in the Crystal Structure of the Apo Form 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 Apo Form of Human H-Ferritin Variant MIC1 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu201 b:27.3 occ:0.50	OE1	A:GLU62	1.8	23.8	1.0
	ND1	A:HIS65	2.2	20.9	1.0
	O	A:HOH336	2.4	24.6	1.0
	OE1	A:GLU27	2.6	24.3	1.0
	O	A:HOH314	2.7	34.2	1.0
	CD	A:GLU62	2.8	25.8	1.0
	O	A:HOH335	2.9	34.8	1.0
	CE1	A:HIS65	3.0	21.1	1.0
	CG	A:HIS65	3.3	21.6	1.0
	OE2	A:GLU62	3.5	27.6	1.0
	CD	A:GLU27	3.5	23.8	1.0
	CG	A:GLU62	3.7	24.4	1.0
	OE2	A:GLU27	3.8	24.1	1.0
	OE1	A:GLN141	3.8	26.8	1.0
	CB	A:HIS65	3.8	21.9	1.0
	NE2	A:HIS65	4.2	21.7	1.0
	O	A:HOH315	4.3	23.6	1.0
	CD2	A:HIS65	4.3	21.3	1.0
	OE1	A:GLU107	4.6	29.1	1.0
	CA	A:GLU62	4.6	23.7	1.0
	CB	A:GLU62	4.7	23.8	1.0
	CG1	A:VAL110	4.8	26.2	1.0
	CD	A:GLN141	4.9	24.6	1.0
	CG	A:GLU27	4.9	21.2	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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