Sodium 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:

Chlorine	(Cl)	3 atoms
Calcium	(Ca)	9 atoms

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Mannose-Binding Protein-A Mutant (Qpdwgh) Complexed with N- Acetyl-D-Galactosamine, PDB code: 1bch:

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


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na 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 2:Na5 b:36.0 occ:1.00 ND1 2:HIS99 2.5 31.2 1.0 O 1:HOH309 2.5 26.0 1.0 ND1 3:HIS99 2.6 31.8 1.0 ND1 1:HIS99 2.6 32.2 1.0 CG 2:HIS99 3.3 27.3 1.0 CE1 3:HIS99 3.3 33.1 1.0 CE1 2:HIS99 3.4 30.2 1.0 CG 3:HIS99 3.4 30.9 1.0 CG 1:HIS99 3.5 29.9 1.0 CE1 1:HIS99 3.5 29.9 1.0 CB 2:HIS99 3.5 26.7 1.0 O 1:HOH301 3.7 28.9 1.0 CB 1:HIS99 3.7 25.6 1.0 CB 3:HIS99 3.8 29.5 1.0 O 3:HOH286 4.0 32.9 1.0 O 2:HOH236 4.2 25.8 1.0 CA 2:HIS99 4.2 26.0 1.0 CA 1:HIS99 4.3 23.4 1.0 NE2 3:HIS99 4.3 32.6 1.0 CD2 2:HIS99 4.4 28.7 1.0 CD2 3:HIS99 4.4 32.0 1.0 NE2 2:HIS99 4.4 31.2 1.0 CA 3:HIS99 4.5 27.3 1.0 NE2 1:HIS99 4.6 33.7 1.0 CD2 1:HIS99 4.6 30.9 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