Chlorine in PDB 1kwy: Rat Mannose Protein A Complexed with Man-A13-Man.

The structure of Rat Mannose Protein A Complexed with Man-A13-Man., PDB code: 1kwy 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 (°)	78.860, 85.250, 98.130, 90.00, 107.34, 90.00
R / Rfree (%)	19.8 / 23.1

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

Calcium

(Ca)

10 atoms

The binding sites of Chlorine atom in the Rat Mannose Protein A Complexed with Man-A13-Man. (pdb code 1kwy). 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 Man-A13-Man., PDB code: 1kwy:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Rat Mannose Protein A 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 Complexed with Man-A13-Man. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl506 b:19.7 occ:1.00 N A:ASP194 3.2 16.6 1.0 O A:HOH687 3.2 15.9 1.0 N A:CYS209 3.3 18.8 1.0 O A:HOH725 3.3 36.4 1.0 CA A:SER208 3.7 18.1 1.0 SG A:CYS209 3.7 18.9 1.0 CB A:ASP194 3.8 17.2 1.0 CA A:ASP194 4.0 15.8 1.0 CB A:CYS209 4.0 18.7 1.0 CA A:GLU193 4.0 17.4 1.0 C A:SER208 4.0 18.8 1.0 C A:GLU193 4.1 18.5 1.0 O A:HOH620 4.2 28.6 1.0 CG A:ASP194 4.2 16.3 1.0 OG A:SER208 4.2 18.2 1.0 O A:GLY192 4.2 16.7 1.0 CA A:CYS209 4.3 20.1 1.0 O A:ILE207 4.3 17.0 1.0 CB A:SER208 4.4 19.8 1.0 OD1 A:ASP194 4.5 15.5 1.0 N A:GLU193 4.5 18.0 1.0 C A:GLY192 4.5 18.3 1.0 N A:CYS195 4.6 15.7 1.0 C A:ASP194 4.7 16.7 1.0 OD2 A:ASP194 4.7 15.0 1.0 NE2 A:GLN210 4.7 45.4 1.0 N A:SER208 4.7 18.1 1.0 O A:HOH698 4.8 59.9 1.0 O A:HOH688 4.9 34.2 1.0 C A:ILE207 4.9 18.4 1.0

Chlorine binding site 2 out of 3 in the Rat Mannose Protein A 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 Complexed with Man-A13-Man. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl606 b:35.3 occ:1.00 O B:HOH715 3.0 31.4 1.0 N B:ASP194 3.1 21.6 1.0 N B:CYS209 3.1 23.7 1.0 O B:HOH667 3.4 43.8 1.0 CA B:SER208 3.6 25.4 1.0 SG B:CYS209 3.7 24.8 1.0 CB B:ASP194 3.7 21.3 1.0 CB B:CYS209 3.8 24.7 1.0 CA B:ASP194 3.9 21.5 1.0 C B:SER208 3.9 26.2 1.0 O B:GLY192 4.0 25.9 1.0 CA B:GLU193 4.0 23.8 1.0 C B:GLU193 4.0 22.6 1.0 CA B:CYS209 4.1 26.0 1.0 OG B:SER208 4.1 26.0 1.0 O B:ILE207 4.2 21.8 1.0 OE1 B:GLN210 4.3 46.0 1.0 CG B:ASP194 4.3 20.3 1.0 N B:CYS195 4.3 21.5 1.0 CB B:SER208 4.4 26.0 1.0 C B:ASP194 4.4 21.8 1.0 C B:GLY192 4.5 26.7 1.0 N B:GLU193 4.5 23.7 1.0 N B:SER208 4.7 24.1 1.0 O B:HOH668 4.7 34.2 1.0 OD1 B:ASP194 4.8 20.8 1.0 OD2 B:ASP194 4.8 17.9 1.0 C B:ILE207 4.8 25.0 1.0

Chlorine binding site 3 out of 3 in the Rat Mannose Protein A 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 Complexed with Man-A13-Man. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl706 b:27.4 occ:1.00 O C:HOH768 3.2 20.5 1.0 N C:ASP194 3.3 19.8 1.0 N C:CYS209 3.3 25.1 1.0 OE1 C:GLN210 3.7 46.9 1.0 CB C:ASP194 3.8 18.6 1.0 SG C:CYS209 3.8 24.8 1.0 CA C:SER208 3.8 23.1 1.0 CB C:CYS209 3.9 23.6 1.0 O C:GLY192 4.0 22.5 1.0 CA C:ASP194 4.1 19.9 1.0 CA C:GLU193 4.1 21.6 1.0 C C:SER208 4.1 23.4 1.0 C C:GLU193 4.1 21.0 1.0 CG C:ASP194 4.2 19.4 1.0 CA C:CYS209 4.2 26.1 1.0 OG C:SER208 4.2 24.8 1.0 C C:GLY192 4.4 24.2 1.0 N C:GLU193 4.4 23.1 1.0 OD1 C:ASP194 4.5 17.3 1.0 O C:ILE207 4.5 24.4 1.0 CB C:SER208 4.5 23.5 1.0 O C:HOH800 4.6 47.4 1.0 N C:CYS195 4.7 19.9 1.0 OD2 C:ASP194 4.7 16.3 1.0 CD C:GLN210 4.8 42.3 1.0 C C:ASP194 4.8 20.3 1.0 N C:SER208 4.9 22.6 1.0 N C:GLN210 4.9 27.6 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