Samarium in PDB 4f3v: Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis

The structure of Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis, PDB code: 4f3v was solved by K.V.Korotkov, T.J.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.230, 92.510, 105.710, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 21.1

The binding sites of Samarium atom in the Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis (pdb code 4f3v). This binding sites where shown within 5.0 Angstroms radius around Samarium atom.
In total 3 binding sites of Samarium where determined in the Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis, PDB code: 4f3v:
Jump to Samarium binding site number: 1; 2; 3;

Samarium binding site 1 out of 3 in the Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 1 of Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm1001 b:42.7 occ:0.15 SG A:CYS109 2.7 31.9 1.0 O A:HOH1311 3.1 47.6 1.0 O A:CYS109 3.3 19.9 1.0 NE2 A:GLN113 3.5 48.9 1.0 CG A:GLN113 3.7 39.6 1.0 CA A:CYS109 3.7 22.5 1.0 CB A:CYS109 3.7 24.3 1.0 C A:CYS109 3.8 22.1 1.0 CB A:ALA112 4.1 25.7 1.0 CD A:GLN113 4.1 44.5 1.0 CB A:ARG52 4.5 44.4 1.0 N A:GLN113 4.7 29.4 1.0 CB A:GLN113 5.0 34.3 1.0

Samarium binding site 2 out of 3 in the Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 2 of Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Sm1001 b:37.7 occ:0.20 SG B:CYS109 2.5 29.4 1.0 O B:CYS109 3.3 23.3 1.0 O B:HOH1250 3.3 51.8 1.0 CB B:CYS109 3.4 24.3 1.0 CA B:CYS109 3.5 22.6 1.0 NE2 B:GLN113 3.6 44.9 1.0 O B:HOH1213 3.6 46.8 1.0 C B:CYS109 3.7 22.9 1.0 CG B:GLN113 3.7 38.5 1.0 SM B:SM1002 3.9 28.8 0.2 CD B:GLN113 4.1 43.7 1.0 CB B:ARG52 4.3 30.2 1.0 CB B:ALA112 4.4 26.7 1.0 CA B:ARG52 4.8 26.6 1.0 N B:GLN113 4.9 31.9 1.0 N B:GLU110 4.9 22.5 1.0 N B:CYS109 4.9 20.0 1.0 O B:HOH1149 5.0 30.0 1.0 O B:HOH1197 5.0 31.4 1.0

Samarium binding site 3 out of 3 in the Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 3 of Crystal Structure of N-Terminal Domain of ECCA1 Atpase From Esx-1 Secretion System of Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Sm1002 b:28.8 occ:0.20 OE2 B:GLU110 2.6 36.1 1.0 SG B:CYS109 2.6 29.4 1.0 O B:HOH1222 3.1 41.9 1.0 C B:CYS109 3.2 22.9 1.0 O B:CYS109 3.2 23.3 1.0 N B:GLU110 3.3 22.5 1.0 CG B:GLN113 3.3 38.5 1.0 CA B:GLU110 3.5 24.9 1.0 CB B:CYS109 3.6 24.3 1.0 CD B:GLU110 3.6 33.5 1.0 SM B:SM1001 3.9 37.7 0.2 CB B:ARG52 3.9 30.2 1.0 CG B:GLU110 3.9 28.7 1.0 CA B:CYS109 4.0 22.6 1.0 CB B:GLN113 4.0 36.1 1.0 CB B:GLU110 4.3 26.3 1.0 CD B:GLN113 4.5 43.7 1.0 C B:GLU110 4.6 24.4 1.0 CD B:ARG52 4.7 41.4 1.0 CA B:ARG52 4.7 26.6 1.0 OE1 B:GLU110 4.8 39.9 1.0 CG B:ARG52 4.8 35.7 1.0 O B:PHE106 4.9 17.5 1.0 O B:GLU110 5.0 23.9 1.0 O B:ARG52 5.0 20.6 1.0

J.M.Wagner, T.J.Evans, K.V.Korotkov. Crystal Structure of the N-Terminal Domain of ECCA1 Atpase From the Esx-1 Secretion System of Mycobacterium Tuberculosis. Proteins V. 82 159 2014.
ISSN: ISSN 0887-3585
PubMed: 23818233
DOI: 10.1002/PROT.24351