Calcium in PDB 2aij: Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr

The structure of Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr, PDB code: 2aij was solved by D.Roeser, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.50 / 1.55
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.640, 109.592, 43.456, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 17.8

The structure of Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Calcium atom in the Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr (pdb code 2aij). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr, PDB code: 2aij:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr within 5.0Å range: probe atom residue distance (Å) B Occ X:Ca1001 b:16.3 occ:1.00 O X:HOH1037 2.3 18.6 1.0 OE2 X:GLU130 2.3 16.8 1.0 O X:ASN293 2.4 14.9 1.0 OE2 X:GLU300 2.4 14.6 1.0 O X:ALA298 2.4 14.6 1.0 O X:GLY296 2.5 13.3 1.0 CD X:GLU300 3.4 16.8 1.0 CD X:GLU130 3.4 17.9 1.0 C X:ALA298 3.5 15.2 1.0 C X:ASN293 3.6 14.7 1.0 C X:GLY296 3.7 14.7 1.0 N X:ALA298 3.7 15.7 1.0 CG X:GLU300 3.7 15.9 1.0 O X:ILE294 3.8 15.9 1.0 CG X:GLU130 4.0 15.8 1.0 C X:ILE294 4.0 14.6 1.0 CA X:ALA298 4.2 15.2 1.0 CA X:ILE294 4.3 14.4 1.0 CB X:ASN297 4.3 14.3 1.0 OE1 X:GLU130 4.4 18.1 1.0 C X:VAL295 4.4 14.1 1.0 O X:GLY332 4.4 15.5 1.0 N X:ILE294 4.4 14.0 1.0 N X:GLY296 4.4 14.3 1.0 OE1 X:GLU300 4.4 14.0 1.0 NH2 X:ARG364 4.4 15.3 1.0 CB X:ASN293 4.5 13.4 1.0 C X:ASN297 4.5 15.6 1.0 N X:ASN297 4.6 13.9 1.0 CA X:ASN293 4.6 14.3 1.0 CA X:GLY296 4.6 14.5 1.0 O X:VAL295 4.6 14.9 1.0 N X:TRP299 4.6 14.2 1.0 N X:VAL295 4.6 14.3 1.0 CA X:ASN297 4.7 14.7 1.0 CB X:ALA298 4.7 16.4 1.0 CA X:VAL295 4.8 13.7 1.0 C X:TRP299 4.9 14.5 1.0 CA X:TRP299 5.0 15.0 1.0

Calcium binding site 2 out of 2 in the Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Formylglycine Generating Enzyme C336S Mutant Covalently Bound to Substrate Peptide Ctpsr within 5.0Å range: probe atom residue distance (Å) B Occ X:Ca1002 b:14.3 occ:1.00 OD1 X:ASN259 2.2 14.5 1.0 O X:ILE260 2.4 15.2 1.0 O X:PHE275 2.4 15.9 1.0 O X:HOH1010 2.4 15.7 1.0 O X:HOH1011 2.4 15.9 1.0 OD1 X:ASP273 2.5 14.8 1.0 OD2 X:ASP273 2.5 14.9 1.0 CG X:ASP273 2.8 16.1 1.0 CG X:ASN259 3.5 15.4 1.0 C X:ILE260 3.5 15.9 1.0 C X:PHE275 3.6 16.0 1.0 N X:ILE260 3.8 13.7 1.0 OE1 X:GLN262 4.1 16.3 1.0 C X:ASN259 4.2 13.9 1.0 CA X:ILE260 4.3 14.6 1.0 CA X:ASN259 4.3 14.2 1.0 ND2 X:ASN259 4.3 15.9 1.0 CB X:ASP273 4.3 15.7 1.0 CA X:PHE275 4.3 15.3 1.0 CB X:PHE275 4.4 15.4 1.0 N X:PHE275 4.4 14.9 1.0 O X:TYR334 4.4 16.2 1.0 CB X:ASN259 4.5 14.0 1.0 NE2 X:GLN262 4.5 15.8 1.0 N X:TRP261 4.5 16.1 1.0 O X:GLN276 4.6 17.6 1.0 N X:GLN276 4.6 17.0 1.0 ND2 X:ASN269 4.6 18.5 1.0 CA X:GLN276 4.7 17.8 1.0 OD1 X:ASN269 4.7 19.3 1.0 CD X:GLN262 4.7 15.4 1.0 CA X:TRP261 4.7 16.0 1.0 C X:GLN276 4.8 16.4 1.0 O X:GLY277 4.9 16.5 1.0 O X:ASN259 4.9 14.4 1.0 CB X:TYR334 4.9 16.2 1.0

D.Roeser, A.Preusser-Kunze, B.Schmidt, K.Gasow, J.G.Wittmann, T.Dierks, K.Von Figura, M.G.Rudolph. A General Binding Mechanism For All Human Sulfatases By the Formylglycine-Generating Enzyme Proc.Natl.Acad.Sci.Usa V. 103 81 2006.
ISSN: ISSN 0027-8424
PubMed: 16368756
DOI: 10.1073/PNAS.0507592102