Calcium in PDB 1lgb: Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety

The structure of Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety, PDB code: 1lgb was solved by Y.Bourne, C.Cambillau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 3.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	63.500, 63.500, 251.900, 90.00, 90.00, 90.00
R / Rfree (%)	21 / n/a

The structure of Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Calcium atom in the Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety (pdb code 1lgb). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety, PDB code: 1lgb:

Calcium binding site 1 out of 1 in the Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:48.8 occ:1.00 OD2 A:ASP121 1.7 31.1 1.0 OD1 A:ASP121 2.1 32.2 1.0 CG A:ASP121 2.1 32.7 1.0 O A:PHE123 2.4 35.6 1.0 OD1 A:ASN125 2.5 23.7 1.0 C A:PHE123 3.5 33.5 1.0 OD1 A:ASP81 3.6 57.1 1.0 CB A:ASP121 3.6 30.9 1.0 OD2 A:ASP129 3.7 38.6 1.0 CG A:ASN125 3.7 27.1 1.0 N A:PHE123 4.0 27.4 1.0 CA A:PHE123 4.2 28.2 1.0 O A:ASP81 4.2 38.8 1.0 CB A:PHE123 4.3 32.0 1.0 OD1 A:ASP129 4.4 39.9 1.0 ND2 A:ASN125 4.4 31.2 1.0 CG A:ASP129 4.4 42.0 1.0 O A:GLY99 4.5 22.2 1.0 N A:TYR124 4.6 34.5 1.0 CG A:ASP81 4.6 53.8 1.0 MN A:MN300 4.6 52.3 1.0 CA A:ASP121 4.6 26.4 1.0 N A:THR122 4.8 31.5 1.0 CB A:ASN125 4.8 30.7 1.0 CA A:TYR124 4.9 38.2 1.0 C A:TYR124 4.9 43.1 1.0 N A:ASN125 4.9 45.6 1.0 C A:ASP121 5.0 30.2 1.0 OD2 A:ASP81 5.0 54.3 1.0

Y.Bourne, J.Mazurier, D.Legrand, P.Rouge, J.Montreuil, G.Spik, C.Cambillau. Structures of A Legume Lectin Complexed with the Human Lactotransferrin N2 Fragment, and with An Isolated Biantennary Glycopeptide: Role of the Fucose Moiety. Structure V. 2 209 1994.
ISSN: ISSN 0969-2126
PubMed: 8069634
DOI: 10.1016/S0969-2126(00)00022-8