Chlorine in PDB 1bch: Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine

The structure of Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine, PDB code: 1bch was solved by A.R.Kolatkar, 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 (°)	80.490, 85.010, 98.710, 90.00, 104.82, 90.00
R / Rfree (%)	21.9 / 25.2

The structure of Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine also contains other interesting chemical elements:

Calcium	(Ca)	9 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine (pdb code 1bch). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine, PDB code: 1bch:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine within 5.0Å range: probe atom residue distance (Å) B Occ 1:Cl4 b:43.6 occ:1.00 O 1:HOH295 3.1 28.0 1.0 N 1:ASP199 3.2 21.2 1.0 O 1:HOH305 3.2 39.5 1.0 N 1:CYS214 3.3 26.0 1.0 O 1:GLY197 3.6 27.8 1.0 CB 1:ASP199 3.7 21.8 1.0 SG 1:CYS214 3.7 27.6 1.0 CA 1:SER213 3.8 25.9 1.0 O 1:HOH284 3.9 52.2 1.0 CA 1:GLU198 3.9 25.9 1.0 CB 1:CYS214 3.9 26.4 1.0 CA 1:ASP199 4.0 22.5 1.0 C 1:GLU198 4.0 23.8 1.0 C 1:SER213 4.0 25.5 1.0 CG 1:ASP199 4.1 21.8 1.0 OE1 1:GLN215 4.1 48.6 1.0 C 1:GLY197 4.1 30.1 1.0 OG 1:SER213 4.1 27.4 1.0 CA 1:CYS214 4.2 27.5 1.0 N 1:GLU198 4.3 27.1 1.0 O 1:ILE212 4.4 22.7 1.0 CB 1:SER213 4.4 28.0 1.0 OD2 1:ASP199 4.4 23.2 1.0 N 1:CYS200 4.6 23.7 1.0 OD1 1:ASP199 4.6 22.0 1.0 C 1:ASP199 4.6 22.5 1.0 N 1:SER213 4.8 26.1 1.0

Chlorine binding site 2 out of 3 in the Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine within 5.0Å range: probe atom residue distance (Å) B Occ 2:Cl4 b:61.5 occ:1.00 N 2:CYS214 3.3 37.8 1.0 N 2:ASP199 3.4 37.8 1.0 O 2:HOH271 3.5 50.8 1.0 O 2:GLY197 3.6 45.5 1.0 CA 2:SER213 3.8 36.7 1.0 SG 2:CYS214 3.8 37.6 1.0 OG 2:SER213 3.9 38.6 1.0 CB 2:ASP199 3.9 37.6 1.0 CB 2:CYS214 4.0 38.2 1.0 C 2:SER213 4.1 37.6 1.0 CA 2:GLU198 4.1 40.1 1.0 CA 2:ASP199 4.1 36.5 1.0 CG 2:ASP199 4.2 37.9 1.0 C 2:GLY197 4.2 45.7 1.0 C 2:GLU198 4.2 39.4 1.0 CA 2:CYS214 4.3 39.6 1.0 CB 2:SER213 4.3 37.5 1.0 OD2 2:ASP199 4.4 39.6 1.0 N 2:GLU198 4.4 43.0 1.0 O 2:ILE212 4.6 35.4 1.0 OD1 2:ASP199 4.7 39.0 1.0 N 2:CYS200 4.8 35.3 1.0 C 2:ASP199 4.8 35.6 1.0 N 2:SER213 4.9 35.8 1.0

Chlorine binding site 3 out of 3 in the Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine within 5.0Å range: probe atom residue distance (Å) B Occ 3:Cl4 b:39.6 occ:1.00 N 3:ASP199 3.1 26.2 1.0 O 3:HOH243 3.2 31.0 1.0 N 3:CYS214 3.3 29.3 1.0 SG 3:CYS214 3.7 28.4 1.0 O 3:GLY197 3.7 30.2 1.0 CB 3:ASP199 3.7 27.0 1.0 CA 3:SER213 3.8 28.0 1.0 CB 3:CYS214 3.9 29.6 1.0 CA 3:ASP199 3.9 27.7 1.0 CA 3:GLU198 4.0 28.9 1.0 C 3:GLU198 4.0 27.4 1.0 C 3:SER213 4.0 29.0 1.0 CG 3:ASP199 4.1 25.3 1.0 CA 3:CYS214 4.2 30.4 1.0 OG 3:SER213 4.2 30.0 1.0 C 3:GLY197 4.2 31.4 1.0 N 3:GLU198 4.4 29.5 1.0 O 3:ILE212 4.4 28.8 1.0 N 3:CYS200 4.5 28.3 1.0 OD1 3:ASP199 4.5 23.9 1.0 CB 3:SER213 4.5 31.0 1.0 C 3:ASP199 4.6 28.4 1.0 OD2 3:ASP199 4.6 24.6 1.0 N 3:SER213 4.9 28.8 1.0 N 3:GLN215 5.0 33.0 1.0

A.R.Kolatkar, A.K.Leung, R.Isecke, R.Brossmer, K.Drickamer, W.I.Weis. Mechanism of N-Acetylgalactosamine Binding to A C-Type Animal Lectin Carbohydrate-Recognition Domain. J.Biol.Chem. V. 273 19502 1998.
ISSN: ISSN 0021-9258
PubMed: 9677372
DOI: 10.1074/JBC.273.31.19502