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

The structure of Rat Mannose Protein A Complexed with A-Me-Fuc., PDB code: 1kww 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 (°)	78.410, 85.560, 98.090, 90.00, 107.00, 90.00
R / Rfree (%)	18.9 / 22.4

The structure of Rat Mannose Protein A Complexed with A-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 A-Me-Fuc. (pdb code 1kww). 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 A-Me-Fuc., PDB code: 1kww:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Rat Mannose Protein A Complexed with A-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 A-Me-Fuc. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:17.7 occ:1.00 O A:HOH746 2.8 40.6 1.0 O A:HOH696 3.1 16.4 1.0 N A:ASP194 3.2 15.3 1.0 N A:CYS209 3.3 16.3 1.0 CA A:SER208 3.7 14.1 1.0 CB A:ASP194 3.7 17.5 1.0 SG A:CYS209 3.8 20.1 1.0 CA A:ASP194 4.0 14.0 1.0 C A:SER208 4.0 15.2 1.0 CB A:CYS209 4.0 15.6 1.0 CA A:GLU193 4.0 15.3 1.0 C A:GLU193 4.1 17.0 1.0 O A:HOH620 4.1 23.8 1.0 OG A:SER208 4.2 14.7 1.0 CG A:ASP194 4.2 15.6 1.0 O A:GLY192 4.2 12.1 1.0 CA A:CYS209 4.3 16.9 1.0 O A:ILE207 4.3 15.5 1.0 CB A:SER208 4.3 14.2 1.0 O A:HOH712 4.4 51.2 1.0 OD1 A:ASP194 4.5 14.1 1.0 N A:GLU193 4.5 14.8 1.0 N A:CYS195 4.6 12.6 1.0 C A:GLY192 4.6 14.3 1.0 C A:ASP194 4.7 12.5 1.0 NE2 A:GLN210 4.7 39.4 1.0 N A:SER208 4.7 13.8 1.0 OD2 A:ASP194 4.7 17.0 1.0 O A:HOH697 4.9 28.5 1.0 C A:ILE207 4.9 14.4 1.0

Chlorine binding site 2 out of 3 in the Rat Mannose Protein A Complexed with A-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 A-Me-Fuc. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl605 b:33.5 occ:1.00 O B:HOH705 2.9 35.0 1.0 N B:ASP194 3.0 18.6 1.0 N B:CYS209 3.2 20.0 1.0 O B:HOH666 3.5 42.5 1.0 SG B:CYS209 3.6 24.7 1.0 CA B:SER208 3.7 18.7 1.0 CB B:ASP194 3.7 18.3 1.0 CA B:ASP194 3.8 19.0 1.0 CB B:CYS209 3.9 21.3 1.0 C B:GLU193 3.9 20.6 1.0 CA B:GLU193 3.9 21.9 1.0 C B:SER208 3.9 20.9 1.0 O B:GLY192 4.0 26.7 1.0 CA B:CYS209 4.1 22.5 1.0 OG B:SER208 4.2 24.6 1.0 OE1 B:GLN210 4.2 42.4 1.0 O B:ILE207 4.2 17.8 1.0 CG B:ASP194 4.3 17.6 1.0 N B:CYS195 4.3 19.2 1.0 C B:ASP194 4.4 19.2 1.0 N B:GLU193 4.5 22.4 1.0 C B:GLY192 4.5 25.7 1.0 CB B:SER208 4.5 20.2 1.0 N B:SER208 4.7 18.4 1.0 OD2 B:ASP194 4.7 15.4 1.0 OD1 B:ASP194 4.8 18.5 1.0 O B:HOH667 4.8 32.1 1.0 C B:ILE207 4.9 19.7 1.0

Chlorine binding site 3 out of 3 in the Rat Mannose Protein A Complexed with A-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 A-Me-Fuc. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl705 b:29.1 occ:1.00 O C:HOH824 3.1 52.8 1.0 N C:CYS209 3.2 21.4 1.0 N C:ASP194 3.2 16.8 1.0 O C:HOH772 3.3 21.6 1.0 SG C:CYS209 3.8 20.7 1.0 CB C:ASP194 3.8 16.5 1.0 CA C:SER208 3.8 20.2 1.0 CB C:CYS209 3.9 21.3 1.0 OE1 C:GLN210 4.0 44.9 1.0 C C:SER208 4.0 20.8 1.0 O C:GLY192 4.0 19.4 1.0 CA C:ASP194 4.0 17.0 1.0 CA C:GLU193 4.0 18.0 1.0 C C:GLU193 4.1 18.2 1.0 CA C:CYS209 4.1 20.4 1.0 OG C:SER208 4.2 21.2 1.0 CG C:ASP194 4.2 16.9 1.0 C C:GLY192 4.4 21.2 1.0 N C:GLU193 4.4 17.3 1.0 O C:ILE207 4.4 20.8 1.0 CB C:SER208 4.5 21.1 1.0 OD1 C:ASP194 4.6 16.1 1.0 N C:CYS195 4.6 16.1 1.0 O C:HOH802 4.7 29.8 1.0 C C:ASP194 4.7 17.2 1.0 O C:HOH816 4.7 38.2 1.0 OD2 C:ASP194 4.8 13.3 1.0 N C:SER208 4.8 18.2 1.0 N C:GLN210 5.0 22.4 1.0 CD C:GLN210 5.0 41.1 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