Calcium in PDB 1ck6: Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase

All present enzymatic activity of Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase:
1.11.1.7;

The structure of Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase, PDB code: 1ck6 was solved by K.Fukuyama, H.Itakura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.90
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	74.410, 74.410, 116.950, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 22.8

The structure of Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase (pdb code 1ck6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase, PDB code: 1ck6:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca346 b:19.2 occ:1.00 OD1 A:ASP57 2.3 19.6 1.0 OD1 A:ASP77 2.5 21.1 1.0 O A:HOH424 2.5 14.9 1.0 O A:ASP57 2.5 18.2 1.0 O A:GLY75 2.6 18.8 1.0 OG A:SER79 2.6 18.7 1.0 O A:HOH425 2.7 21.1 1.0 CG A:ASP57 3.4 19.5 1.0 C A:ASP57 3.4 19.5 1.0 CG A:ASP77 3.5 22.0 1.0 CB A:SER79 3.8 17.0 1.0 CA A:ASP57 3.8 19.4 1.0 C A:GLY75 3.8 18.9 1.0 OD2 A:ASP77 3.9 23.5 1.0 N A:SER79 4.0 17.0 1.0 N A:ASP77 4.1 18.3 1.0 CB A:ASP57 4.2 18.5 1.0 O A:HOH363 4.2 20.9 1.0 OD2 A:ASP57 4.2 18.0 1.0 N A:GLY75 4.4 20.3 1.0 CA A:SER79 4.4 18.0 1.0 N A:GLY78 4.5 15.1 1.0 O A:GLY60 4.5 21.6 1.0 CA A:GLY75 4.5 18.9 1.0 N A:ALA58 4.5 18.7 1.0 N A:ILE80 4.6 19.2 1.0 CB A:ASP77 4.7 18.3 1.0 CA A:ASP77 4.8 18.4 1.0 OE2 A:GLU87 4.8 19.0 1.0 N A:ALA76 4.8 18.4 1.0 OE1 A:GLU87 4.9 20.1 1.0 C A:SER79 4.9 19.9 1.0 C A:ASP77 4.9 17.6 1.0 CA A:ALA76 5.0 18.8 1.0 O A:HIS56 5.0 18.2 1.0 CB A:SER148 5.0 21.1 1.0 CA A:ALA58 5.0 19.0 1.0 C A:GLY74 5.0 22.3 1.0

Calcium binding site 2 out of 2 in the Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Binding Mode of Salicylhydroxamic Acid to Arthromyces Ramosus Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca347 b:18.0 occ:1.00 O A:THR204 2.4 17.7 1.0 O A:SER185 2.5 17.3 1.0 OD1 A:ASP209 2.5 15.7 1.0 OD2 A:ASP202 2.5 15.5 1.0 OG A:SER185 2.5 15.7 1.0 OG1 A:THR204 2.5 16.6 1.0 O A:VAL207 2.6 16.8 1.0 OD1 A:ASP202 2.7 16.7 1.0 CG A:ASP202 3.0 17.8 1.0 C A:THR204 3.3 17.6 1.0 C A:SER185 3.4 16.6 1.0 CG A:ASP209 3.5 14.6 1.0 CB A:THR204 3.6 14.9 1.0 CB A:SER185 3.6 15.3 1.0 CA A:SER185 3.7 15.0 1.0 C A:VAL207 3.8 16.5 1.0 OD2 A:ASP209 3.8 14.4 1.0 CA A:THR204 3.9 15.9 1.0 N A:THR204 4.1 17.9 1.0 N A:ASP209 4.2 16.6 1.0 N A:PRO205 4.3 18.0 1.0 N A:VAL207 4.3 16.4 1.0 O A:ASP209 4.5 16.4 1.0 CB A:ASP202 4.5 15.0 1.0 O A:HOH515 4.5 18.6 1.0 CA A:VAL207 4.6 15.8 1.0 CA A:PRO205 4.6 19.8 1.0 N A:LEU186 4.6 16.5 1.0 CB A:GLN211 4.6 14.7 1.0 CB A:ASP209 4.7 14.4 1.0 CB A:VAL207 4.7 14.6 1.0 N A:PHE208 4.7 16.6 1.0 CA A:ASP209 4.8 15.4 1.0 CA A:PHE208 4.8 16.3 1.0 CD1 A:LEU186 4.8 16.5 1.0 CG2 A:THR204 4.9 14.2 1.0 C A:ASP209 4.9 17.3 1.0 C A:PRO205 5.0 19.7 1.0

K.Tsukamoto, H.Itakura, K.Sato, K.Fukuyama, S.Miura, S.Takahashi, H.Ikezawa, T.Hosoya. Binding of Salicylhydroxamic Acid and Several Aromatic Donor Molecules to Arthromyces Ramosus Peroxidase, Investigated By X-Ray Crystallography, Optical Difference Spectroscopy, uc(Nmr) Relaxation, Molecular Dynamics, and Kinetics. Biochemistry V. 38 12558 1999.
ISSN: ISSN 0006-2960
PubMed: 10504224
DOI: 10.1021/BI982925L