Calcium in PDB 1z0w: Crystal Structure of A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution

All present enzymatic activity of Crystal Structure of A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution:
3.4.21.53;

The structure of Crystal Structure of A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution, PDB code: 1z0w was solved by I.Botos, E.E.Melnikov, S.Cherry, S.Kozlov, O.V.Makhovskaya, J.E.Tropea, A.Gustchina, T.V.Rotanova, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.20
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	84.470, 84.470, 41.500, 90.00, 90.00, 120.00
R / Rfree (%)	13.7 / 18.1

The binding sites of Calcium atom in the Crystal Structure of A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution (pdb code 1z0w). 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 A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution, PDB code: 1z0w:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution


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 A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca901 b:18.7 occ:1.00 O A:HOH1015 2.3 26.2 1.0 O A:HOH1013 2.3 20.4 1.0 O A:HOH1014 2.4 19.3 1.0 O A:HOH1012 2.4 25.9 1.0 O A:HOH1016 2.5 26.9 1.0 OE2 A:GLU585 2.5 20.3 1.0 OE1 A:GLU585 2.5 24.1 1.0 O A:HOH1011 2.7 28.7 1.0 CD A:GLU585 2.9 19.3 1.0 O A:HOH1212 4.1 45.8 1.0 CG A:GLU585 4.4 16.9 1.0 O A:HOH1003 4.5 19.8 1.0 O A:HOH1090 4.6 32.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution


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 A. Fulgidus Lon Proteolytic Domain at 1.2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca902 b:17.6 occ:1.00 O A:VAL586 2.3 14.5 1.0 O A:HOH1002 2.3 20.8 1.0 O A:HOH1004 2.4 21.8 1.0 O A:HOH1001 2.4 23.3 1.0 O A:HOH1005 2.4 21.0 1.0 O A:HOH1003 2.5 19.8 1.0 C A:VAL586 3.5 13.3 1.0 N A:VAL586 4.2 13.4 1.0 O A:HOH1082 4.3 33.9 1.0 CA A:VAL586 4.3 13.3 1.0 OE2 A:GLU585 4.3 20.3 1.0 CD A:PRO588 4.4 15.9 1.0 N A:ILE587 4.5 13.2 1.0 CB A:VAL586 4.6 14.7 1.0 CA A:ILE587 4.7 13.6 1.0 O A:HOH1240 4.8 60.1 1.0 CG A:GLU585 4.9 16.9 1.0

I.Botos, E.E.Melnikov, S.Cherry, S.Kozlov, O.V.Makhovskaya, J.E.Tropea, A.Gustchina, T.V.Rotanova, A.Wlodawer. Atomic-Resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus Fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases J.Mol.Biol. V. 351 144 2005.
ISSN: ISSN 0022-2836
PubMed: 16002085
DOI: 10.1016/J.JMB.2005.06.008