Chlorine in PDB 1kwz: Rat Mannose Protein A (H189V) Complexed with Man-A13-Man

The structure of Rat Mannose Protein A (H189V) Complexed with Man-A13-Man, PDB code: 1kwz was solved by K.K.Ng, A.R.Kolatkar, S.Park-Snyder, H.Feinberg, D.A.Clark, K.Drickamer, W.I.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.350, 85.050, 98.160, 90.00, 106.90, 90.00
R / Rfree (%)	22.3 / 25.2

The structure of Rat Mannose Protein A (H189V) Complexed with Man-A13-Man also contains other interesting chemical elements:

Calcium

(Ca)

9 atoms

The binding sites of Chlorine atom in the Rat Mannose Protein A (H189V) Complexed with Man-A13-Man (pdb code 1kwz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Rat Mannose Protein A (H189V) Complexed with Man-A13-Man, PDB code: 1kwz:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Rat Mannose Protein A (H189V) Complexed with Man-A13-Man


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Rat Mannose Protein A (H189V) Complexed with Man-A13-Man within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl506 b:23.8 occ:1.00 O A:HOH517 3.2 23.0 1.0 N A:ASP194 3.2 18.9 1.0 N A:CYS209 3.2 21.6 1.0 CA A:SER208 3.7 19.2 1.0 CB A:ASP194 3.7 18.1 1.0 SG A:CYS209 3.7 22.2 1.0 C A:SER208 4.0 19.0 1.0 CA A:ASP194 4.0 15.2 1.0 CB A:CYS209 4.0 22.6 1.0 OG A:SER208 4.0 18.4 1.0 CA A:GLU193 4.1 18.4 1.0 C A:GLU193 4.1 20.4 1.0 O A:HOH576 4.1 41.5 1.0 CG A:ASP194 4.2 12.9 1.0 O A:GLY192 4.2 20.2 1.0 CA A:CYS209 4.2 22.9 1.0 NE2 A:GLN210 4.3 41.5 1.0 CB A:SER208 4.3 19.0 1.0 O A:ILE207 4.3 15.0 1.0 OD1 A:ASP194 4.5 13.2 1.0 N A:CYS195 4.5 16.5 1.0 C A:ASP194 4.6 16.7 1.0 C A:GLY192 4.6 19.9 1.0 N A:GLU193 4.6 18.1 1.0 OD2 A:ASP194 4.7 13.7 1.0 N A:SER208 4.7 17.5 1.0 C A:ILE207 5.0 16.3 1.0

Chlorine binding site 2 out of 3 in the Rat Mannose Protein A (H189V) Complexed with Man-A13-Man


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Rat Mannose Protein A (H189V) Complexed with Man-A13-Man within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl606 b:45.6 occ:1.00 N B:ASP194 3.0 22.5 1.0 N B:CYS209 3.1 25.2 1.0 O B:HOH688 3.4 43.5 1.0 CA B:SER208 3.5 25.4 1.0 SG B:CYS209 3.7 27.4 1.0 CB B:ASP194 3.7 21.8 1.0 CA B:ASP194 3.8 23.4 1.0 C B:SER208 3.8 25.1 1.0 CA B:GLU193 3.8 28.5 1.0 OG B:SER208 3.9 28.0 1.0 C B:GLU193 3.9 25.0 1.0 CB B:CYS209 3.9 27.3 1.0 O B:GLY192 4.0 30.4 1.0 O B:ILE207 4.0 24.7 1.0 CA B:CYS209 4.1 25.5 1.0 CB B:SER208 4.2 26.5 1.0 N B:CYS195 4.3 22.8 1.0 N B:GLU193 4.4 29.7 1.0 CG B:ASP194 4.4 20.5 1.0 OE1 B:GLN210 4.4 51.6 1.0 C B:GLY192 4.4 33.4 1.0 C B:ASP194 4.4 23.4 1.0 N B:SER208 4.6 24.8 1.0 C B:ILE207 4.7 24.2 1.0 OD2 B:ASP194 4.8 19.1 1.0 OD1 B:ASP194 4.9 28.5 1.0 O B:HOH657 4.9 35.9 1.0

Chlorine binding site 3 out of 3 in the Rat Mannose Protein A (H189V) Complexed with Man-A13-Man


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Rat Mannose Protein A (H189V) Complexed with Man-A13-Man within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl706 b:26.5 occ:1.00 N C:CYS209 3.2 24.6 1.0 O C:HOH715 3.2 21.9 1.0 N C:ASP194 3.3 21.2 1.0 CA C:SER208 3.8 25.5 1.0 SG C:CYS209 3.8 24.3 1.0 CB C:ASP194 3.8 23.3 1.0 OE1 C:GLN210 3.8 41.8 1.0 CB C:CYS209 3.9 24.7 1.0 C C:SER208 4.0 25.1 1.0 CA C:ASP194 4.1 22.1 1.0 O C:GLY192 4.1 24.6 1.0 CA C:GLU193 4.1 21.9 1.0 CG C:ASP194 4.2 25.0 1.0 OG C:SER208 4.2 27.5 1.0 C C:GLU193 4.2 20.7 1.0 CA C:CYS209 4.2 26.5 1.0 O C:ILE207 4.4 21.3 1.0 CB C:SER208 4.5 25.5 1.0 OD1 C:ASP194 4.5 23.9 1.0 C C:GLY192 4.5 24.0 1.0 N C:GLU193 4.5 21.8 1.0 N C:CYS195 4.7 22.6 1.0 OD2 C:ASP194 4.7 22.9 1.0 C C:ASP194 4.7 21.9 1.0 O C:HOH772 4.7 45.5 1.0 CD C:GLN210 4.8 40.1 1.0 N C:SER208 4.8 23.4 1.0 NE2 C:GLN210 5.0 40.5 1.0

K.K.Ng, A.R.Kolatkar, S.Park-Snyder, H.Feinberg, D.A.Clark, K.Drickamer, W.I.Weis. Orientation of Bound Ligands in Mannose-Binding Proteins. Implications For Multivalent Ligand Recognition. J.Biol.Chem. V. 277 16088 2002.
ISSN: ISSN 0021-9258
PubMed: 11850428
DOI: 10.1074/JBC.M200493200