Calcium in PDB 1z0b: Crystal Structure of A. Fulgidus Lon Proteolytic Domain E506A Mutant

All present enzymatic activity of Crystal Structure of A. Fulgidus Lon Proteolytic Domain E506A Mutant:
3.4.21.53;

The structure of Crystal Structure of A. Fulgidus Lon Proteolytic Domain E506A Mutant, PDB code: 1z0b 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 / 1.55
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	83.260, 83.260, 41.170, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 20.7

The binding sites of Calcium atom in the Crystal Structure of A. Fulgidus Lon Proteolytic Domain E506A Mutant (pdb code 1z0b). 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 E506A Mutant, PDB code: 1z0b:
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 E506A Mutant


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 E506A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca901 b:49.6 occ:1.00 OE1 A:GLU585 2.3 38.8 1.0 O A:HOH71 2.5 47.5 1.0 O A:HOH140 2.9 82.7 1.0 O A:HOH54 3.0 44.5 1.0 O A:HOH84 3.1 53.8 1.0 O A:HOH101 3.1 58.1 1.0 CD A:GLU585 3.5 38.2 1.0 O A:HOH135 3.8 63.3 1.0 OE2 A:GLU585 4.1 44.4 1.0 CG A:GLU585 4.7 31.6 1.0 CB A:GLU585 4.7 28.8 1.0 CA A:GLU585 4.9 27.8 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of A. Fulgidus Lon Proteolytic Domain E506A Mutant


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 E506A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca902 b:37.2 occ:1.00 O A:HOH38 2.3 39.8 1.0 O A:VAL586 2.3 26.6 1.0 O A:HOH160 2.4 43.2 1.0 O A:HOH109 2.5 48.5 1.0 OE2 A:GLU585 2.6 44.4 1.0 C A:VAL586 3.5 26.9 1.0 CD A:GLU585 3.6 38.2 1.0 N A:VAL586 4.1 27.4 1.0 CA A:VAL586 4.3 27.0 1.0 O A:HOH101 4.3 58.1 1.0 CG A:GLU585 4.4 31.6 1.0 OE1 A:GLU585 4.4 38.8 1.0 N A:ILE587 4.5 26.4 1.0 O A:HOH86 4.5 51.4 1.0 CD A:PRO588 4.5 27.7 1.0 CA A:ILE587 4.6 26.8 1.0 CB A:VAL586 4.7 27.2 1.0 O A:HOH140 4.7 82.7 1.0 C A:GLU585 5.0 27.5 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