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

Protein crystallography data

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

Other elements in 1bch:

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

Sodium Binding Sites:

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 1bch

Go back to Sodium Binding Sites List in 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

Reference:

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
Page generated: Tue Dec 15 05:22:07 2020

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