Chlorine in PDB 1kwx: Rat Mannose Protein A Complexed with B-Me-Fuc.

The structure of Rat Mannose Protein A Complexed with B-Me-Fuc., PDB code: 1kwx 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 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	78.480, 85.430, 97.800, 90.00, 107.37, 90.00
R / Rfree (%)	20 / 22.9

The structure of Rat Mannose Protein A Complexed with B-Me-Fuc. also contains other interesting chemical elements:

Calcium

(Ca)

10 atoms

The binding sites of Chlorine atom in the Rat Mannose Protein A Complexed with B-Me-Fuc. (pdb code 1kwx). 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 Complexed with B-Me-Fuc., PDB code: 1kwx:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Rat Mannose Protein A Complexed with B-Me-Fuc.


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 Complexed with B-Me-Fuc. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:20.2 occ:1.00 O A:HOH745 3.1 52.2 1.0 O A:HOH695 3.1 18.8 1.0 O A:HOH744 3.2 31.0 1.0 N A:ASP194 3.2 14.1 1.0 N A:CYS209 3.3 17.1 1.0 CA A:SER208 3.7 17.3 1.0 SG A:CYS209 3.8 20.2 1.0 CB A:ASP194 3.8 16.8 1.0 CB A:CYS209 4.0 19.6 1.0 CA A:ASP194 4.0 14.5 1.0 C A:SER208 4.0 16.8 1.0 CA A:GLU193 4.0 16.0 1.0 C A:GLU193 4.1 17.2 1.0 OG A:SER208 4.2 19.0 1.0 O A:GLY192 4.2 16.3 1.0 CA A:CYS209 4.3 19.9 1.0 CG A:ASP194 4.3 15.0 1.0 O A:ILE207 4.3 15.5 1.0 O A:HOH620 4.3 28.8 1.0 CB A:SER208 4.4 18.2 1.0 NE2 A:GLN210 4.4 43.5 1.0 N A:GLU193 4.5 15.2 1.0 C A:GLY192 4.6 16.7 1.0 N A:CYS195 4.6 13.8 1.0 OD1 A:ASP194 4.6 12.7 1.0 C A:ASP194 4.7 15.9 1.0 N A:SER208 4.8 17.5 1.0 OD2 A:ASP194 4.9 16.7 1.0 O A:HOH708 4.9 50.3 1.0 C A:ILE207 4.9 16.6 1.0

Chlorine binding site 2 out of 3 in the Rat Mannose Protein A Complexed with B-Me-Fuc.


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 Complexed with B-Me-Fuc. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl605 b:37.6 occ:1.00 N B:ASP194 3.0 16.8 1.0 O B:HOH696 3.1 39.4 1.0 N B:CYS209 3.3 24.0 1.0 CB B:ASP194 3.7 19.9 1.0 SG B:CYS209 3.7 25.3 1.0 CA B:SER208 3.7 23.4 1.0 CA B:ASP194 3.8 20.7 1.0 CB B:CYS209 4.0 22.3 1.0 C B:GLU193 4.0 19.5 1.0 C B:SER208 4.0 24.8 1.0 CA B:GLU193 4.0 23.6 1.0 O B:GLY192 4.1 30.9 1.0 OG B:SER208 4.2 26.4 1.0 CA B:CYS209 4.2 24.8 1.0 OE1 B:GLN210 4.3 51.4 1.0 CG B:ASP194 4.3 21.4 1.0 O B:ILE207 4.3 21.9 1.0 N B:CYS195 4.3 22.2 1.0 C B:ASP194 4.4 21.7 1.0 C B:GLY192 4.5 31.6 1.0 N B:GLU193 4.5 27.9 1.0 CB B:SER208 4.5 22.8 1.0 O B:HOH665 4.7 40.7 1.0 OD2 B:ASP194 4.7 19.2 1.0 N B:SER208 4.8 23.1 1.0 OD1 B:ASP194 4.8 22.4 1.0 C B:ILE207 4.9 23.8 1.0

Chlorine binding site 3 out of 3 in the Rat Mannose Protein A Complexed with B-Me-Fuc.


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 Complexed with B-Me-Fuc. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl705 b:23.8 occ:1.00 O C:HOH771 3.2 19.2 1.0 N C:CYS209 3.2 20.5 1.0 N C:ASP194 3.2 16.8 1.0 CA C:SER208 3.8 20.0 1.0 CB C:ASP194 3.8 15.5 1.0 SG C:CYS209 3.8 24.4 1.0 CB C:CYS209 3.9 17.2 1.0 CA C:GLU193 4.0 16.4 1.0 O C:GLY192 4.0 19.1 1.0 C C:SER208 4.0 18.1 1.0 C C:GLU193 4.0 17.2 1.0 CA C:ASP194 4.1 16.1 1.0 OG C:SER208 4.2 19.7 1.0 CA C:CYS209 4.2 22.0 1.0 CG C:ASP194 4.3 18.1 1.0 N C:GLU193 4.3 15.9 1.0 C C:GLY192 4.3 19.5 1.0 CB C:SER208 4.4 17.8 1.0 O C:ILE207 4.5 18.1 1.0 OD1 C:ASP194 4.6 17.4 1.0 O C:HOH811 4.6 35.9 1.0 N C:CYS195 4.7 16.9 1.0 OD2 C:ASP194 4.8 13.4 1.0 C C:ASP194 4.8 15.8 1.0 N C:SER208 4.8 16.6 1.0 O C:HOH798 4.8 57.4 1.0 N C:GLN210 5.0 22.6 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