Calcium in PDB 5ssz: 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;

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 / Rfree (%)	13.1 / 14.2

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

Copper

(Cu)

1 atom

The binding sites of Calcium 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 Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Wild-Type Human Formylglycine Generating Enzyme Bound to Cu(I), PDB code: 5ssz:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 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 Calcium with other atoms in the Ca 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:Ca402 b:5.6 occ:1.00 OE2 A:GLU130 2.3 6.0 1.0 O A:HOH619 2.3 6.5 1.0 O A:ASN293 2.3 6.2 1.0 OE2 A:GLU300 2.3 6.0 1.0 O A:ALA298 2.4 5.8 1.0 O A:GLY296 2.4 5.9 1.0 CD A:GLU300 3.3 5.9 1.0 CD A:GLU130 3.4 5.8 1.0 C A:ALA298 3.5 5.8 1.0 C A:ASN293 3.6 5.9 1.0 C A:GLY296 3.6 5.7 1.0 CG A:GLU300 3.7 7.1 1.0 N A:ALA298 3.7 6.0 1.0 O A:ILE294 3.9 6.6 1.0 CG A:GLU130 3.9 6.4 1.0 C A:ILE294 4.1 5.7 1.0 CA A:ALA298 4.1 6.4 1.0 CA A:ILE294 4.3 6.2 0.5 O A:GLY332 4.3 6.8 1.0 CB A:ASN297 4.3 6.0 1.0 CA A:ILE294 4.3 6.2 0.5 N A:GLY296 4.4 6.0 1.0 OE1 A:GLU130 4.4 7.3 1.0 CB A:ASN293 4.4 5.9 1.0 N A:ILE294 4.4 5.9 1.0 C A:VAL295 4.4 5.9 1.0 NH2 A:ARG364 4.5 6.2 1.0 OE1 A:GLU300 4.5 6.3 1.0 C A:ASN297 4.5 5.9 1.0 N A:ASN297 4.6 5.7 1.0 CA A:ASN293 4.6 6.0 1.0 N A:TRP299 4.6 5.8 1.0 CA A:GLY296 4.6 6.2 1.0 CA A:ASN297 4.6 6.1 1.0 O A:VAL295 4.7 6.5 1.0 N A:VAL295 4.7 6.1 1.0 CB A:ALA298 4.7 7.5 1.0 CA A:VAL295 4.8 6.1 1.0 C A:TRP299 4.9 5.8 1.0 CA A:TRP299 4.9 6.0 1.0

Calcium binding site 2 out of 2 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 Calcium with other atoms in the Ca binding site number 2 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:Ca403 b:6.0 occ:1.00 OD1 A:ASN259 2.3 6.4 1.0 O A:ILE260 2.3 6.8 1.0 O A:PHE275 2.3 7.0 1.0 O A:HOH545 2.4 6.7 1.0 O A:HOH571 2.4 6.9 1.0 OD2 A:ASP273 2.5 6.7 1.0 OD1 A:ASP273 2.5 6.7 1.0 CG A:ASP273 2.8 6.3 1.0 C A:ILE260 3.5 6.0 1.0 C A:PHE275 3.6 6.2 1.0 CG A:ASN259 3.6 5.9 1.0 N A:ILE260 3.8 6.0 1.0 OE1 A:GLN262 4.1 7.3 1.0 C A:ASN259 4.2 5.8 1.0 CA A:ILE260 4.3 6.2 1.0 CA A:ASN259 4.3 6.1 1.0 CB A:ASP273 4.3 7.0 1.0 CA A:PHE275 4.3 6.3 1.0 N A:PHE275 4.4 6.5 1.0 ND2 A:ASN259 4.4 6.2 1.0 NE2 A:GLN262 4.4 7.2 1.0 CB A:PHE275 4.5 7.0 1.0 CB A:ASN259 4.5 6.4 1.0 N A:TRP261 4.5 6.5 1.0 N A:GLN276 4.5 6.3 0.5 O A:TYR334 4.5 6.6 1.0 CA A:GLN276 4.6 6.4 0.5 O A:GLN276 4.6 7.5 0.5 O A:GLN276 4.6 8.0 0.5 N A:GLN276 4.6 7.1 0.5 CD A:GLN262 4.6 7.1 1.0 ND2 A:ASN269 4.6 9.4 1.0 OD1 A:ASN269 4.6 10.2 1.0 CA A:TRP261 4.7 7.1 1.0 CA A:GLN276 4.8 8.2 0.5 C A:GLN276 4.8 6.3 0.5 C A:GLN276 4.9 7.5 0.5 O A:GLY277 4.9 7.1 1.0 CB A:TYR334 5.0 6.6 1.0 O A:ASN259 5.0 6.1 1.0

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