Chlorine in PDB 1vcl: Crystal Structure of Hemolytic Lectin Cel-III

The structure of Crystal Structure of Hemolytic Lectin Cel-III, PDB code: 1vcl was solved by T.Uchida, T.Yamasaki, S.Eto, H.Sugawara, G.Kurisu, A.Nakagawa, M.Kusunoki, T.Hatakeyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.17 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.420, 65.370, 126.020, 90.00, 98.18, 90.00
R / Rfree (%)	16.5 / 20.1

The structure of Crystal Structure of Hemolytic Lectin Cel-III also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Calcium	(Ca)	10 atoms

The binding sites of Chlorine atom in the Crystal Structure of Hemolytic Lectin Cel-III (pdb code 1vcl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Hemolytic Lectin Cel-III, PDB code: 1vcl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Hemolytic Lectin Cel-III


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Hemolytic Lectin Cel-III within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1201 b:45.3 occ:1.00 N A:SER213 3.0 24.8 1.0 N A:ASP214 3.2 23.8 1.0 CG A:ASP214 3.5 28.0 1.0 OD1 A:ASP214 3.6 26.9 1.0 CA A:GLY212 3.7 25.4 1.0 CB A:ASP214 3.8 25.4 1.0 OD2 A:ASP214 3.8 32.6 1.0 C A:GLY212 3.8 24.6 1.0 OG A:SER213 3.9 26.6 1.0 CA A:SER213 3.9 24.4 1.0 C A:SER213 4.0 24.2 1.0 CA A:ASP214 4.0 24.4 1.0 O A:HOH1528 4.2 45.0 1.0 O A:GLU211 4.4 24.1 1.0 CB A:SER213 4.5 25.2 1.0 O A:HOH1304 4.8 19.6 1.0 N A:GLY212 4.8 25.3 1.0 O A:GLY212 5.0 23.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Hemolytic Lectin Cel-III


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Hemolytic Lectin Cel-III within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl2201 b:44.8 occ:1.00 N B:SER213 3.1 23.4 1.0 N B:ASP214 3.3 22.2 1.0 CG B:ASP214 3.5 24.5 1.0 OD1 B:ASP214 3.6 20.6 1.0 CA B:GLY212 3.7 22.6 1.0 CB B:ASP214 3.8 22.8 1.0 OD2 B:ASP214 3.8 27.9 1.0 C B:GLY212 3.8 22.1 1.0 OG B:SER213 4.0 28.5 1.0 CA B:SER213 4.1 23.3 1.0 C B:SER213 4.1 23.1 1.0 CA B:ASP214 4.1 22.1 1.0 O B:GLU211 4.3 20.2 1.0 O B:HOH2329 4.6 30.7 1.0 CB B:SER213 4.7 25.1 1.0 O B:HOH2368 4.8 41.9 1.0 N B:GLY212 4.8 22.0 1.0 O B:HOH2202 4.8 20.2 1.0 C B:GLU211 5.0 20.8 1.0

T.Uchida, T.Yamasaki, S.Eto, H.Sugawara, G.Kurisu, A.Nakagawa, M.Kusunoki, T.Hatakeyama. Crystal Structure of the Hemolytic Lectin Cel-III Isolated From the Marine Invertebrate Cucumaria Echinata: Implications of Domain Structure For Its Membrane Pore-Formation Mechanism J.Biol.Chem. V. 279 37133 2004.
ISSN: ISSN 0021-9258
PubMed: 15194688
DOI: 10.1074/JBC.M404065200