Chlorine in PDB 3svi: Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion

The structure of Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion, PDB code: 3svi was solved by A.U.Singer, A.Stein, X.Xu, H.Cui, A.Joachimiak, A.M.Edwards, A.Savchenko, Midwest Center For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.62 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.277, 57.277, 55.658, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 21.8

The structure of Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion (pdb code 3svi). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion, PDB code: 3svi:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl234 b:69.5 occ:1.00 NH2 A:ARG164 3.5 24.1 1.0 NH1 A:ARG164 3.7 21.8 1.0 O A:HOH61 3.7 39.5 1.0 CZ A:ARG164 4.1 24.5 1.0

Chlorine binding site 2 out of 4 in the Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl3 b:49.1 occ:1.00 ND2 A:ASN184 3.0 45.7 1.0 NH1 A:ARG180 3.9 36.0 1.0 CG A:ASN184 4.0 38.2 1.0 CD A:ARG180 4.1 46.3 1.0 CG A:ARG180 4.2 44.1 1.0 OD1 A:ASN184 4.3 36.5 1.0 CZ A:ARG180 4.9 42.3 1.0 NE A:ARG180 5.0 48.5 1.0

Chlorine binding site 3 out of 4 in the Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl4 b:56.0 occ:1.00 O A:HOH33 3.1 36.9 1.0 CD A:ARG145 3.4 32.8 1.0 CA A:ALA142 3.9 16.9 1.0 CB A:ARG145 4.2 15.2 1.0 N A:ALA142 4.2 16.8 1.0 CG A:ARG145 4.3 25.4 1.0 O A:HOH132 4.3 31.9 1.0 CD1 A:LEU204 4.4 14.8 1.0 CB A:LEU204 4.4 13.6 1.0 CB A:ALA142 4.4 16.1 1.0 NE A:ARG145 4.5 29.4 1.0 O A:GLY141 4.5 15.1 1.0 C A:GLY141 4.5 18.6 1.0 O A:THR140 4.7 42.9 1.0 CG A:LEU204 4.7 12.3 1.0 O A:HOH121 4.7 17.5 1.0 CD2 A:LEU204 4.7 12.0 1.0 NH1 A:ARG145 4.7 49.4 1.0 O A:HOH74 5.0 24.0 1.0

Chlorine binding site 4 out of 4 in the Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of the Pto-Binding Domain of Hoppmal Generated By Limited Thermolysin Digestion within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl235 b:66.5 occ:1.00 NH2 A:ARG145 3.4 44.5 1.0 NH1 A:ARG145 3.7 49.4 1.0 CZ A:ARG145 4.0 43.4 1.0 O A:HOH74 4.9 24.0 1.0

A.U.Singer, B.Wu, A.Yee, S.Houliston, X.Xu, H.Cui, T.Skarina, M.Garcia, A.Semesi, C.H.Arrowsmith, A.Savchenko. Structural Analysis of Hoppmal Reveals the Presence of A Second Adaptor Domain Common to the Hopab Family of Pseudomonas Syringae Type III Effectors. Biochemistry V. 51 1 2012.
ISSN: ISSN 0006-2960
PubMed: 22191472
DOI: 10.1021/BI2013883