Copper in PDB 5ssz: Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I)

Enzymatic activity of Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I)

All present enzymatic activity of Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I):
1.8.3.7;

Protein crystallography data

The structure of Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I), PDB code: 5ssz was solved by K.Radhakrishnan, L.Schlotawa, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	55.01 / 1.02
*Space group*	P 2 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	43.513, 62.024, 110.021, 90, 90, 90
*R / R_free (%)*	13.1 / 14.2

Other elements in 5ssz:

The structure of Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I) also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I) (pdb code 5ssz). 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 Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I), PDB code: 5ssz:

Copper binding site 1 out of 1 in 5ssz

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Copper Binding Sites List in 5ssz

Copper binding site 1 out of 1 in the Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I)

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 Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu400 b:7.8 occ:1.00	SG	A:CYS336	2.1	11.9	1.0
	SG	A:CYS341	2.2	13.8	1.0
	O	A:CYS341	2.8	10.4	1.0
	CB	A:CYS341	3.0	12.1	1.0
	CB	A:CYS336	3.1	9.3	1.0
	O	A:HOH567	3.4	11.7	1.0
	C	A:CYS341	3.4	10.2	1.0
	CA	A:CYS336	3.6	7.8	1.0
	CB	A:ARG343	3.6	9.1	1.0
	CA	A:CYS341	3.8	11.3	1.0
	N	A:ARG343	3.8	8.1	1.0
	O	A:HOH812	4.2	26.1	1.0
	CA	A:ARG343	4.2	7.8	1.0
	O	A:HOH610	4.2	17.2	1.0
	CZ2	A:TRP299	4.3	8.8	1.0
	CG	A:ARG343	4.3	9.7	1.0
	N	A:CYS336	4.4	7.5	1.0
	N	A:TYR342	4.4	10.1	1.0
	C	A:ARG343	4.7	7.7	1.0
	CD	A:ARG343	4.7	10.8	1.0
	CA	A:GLY332	4.7	6.8	1.0
	C	A:CYS336	4.7	7.4	1.0
	N	A:HIS337	4.8	8.8	1.0
	NE1	A:TRP299	4.9	8.4	1.0
	CE2	A:TRP299	4.9	7.9	1.0
	C	A:TYR342	4.9	8.5	1.0
	NH1	A:ARG343	5.0	14.0	1.0

Reference:

K.Radhakrishnan, L.Schlotawa, M.G.Rudolph. Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I) To Be Published.

Page generated: Mon Jul 14 05:23:47 2025

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