Calcium in PDB 1hfy: Alpha-Lactalbumin

All present enzymatic activity of Alpha-Lactalbumin:
2.4.1.22;

The structure of Alpha-Lactalbumin, PDB code: 1hfy was solved by A.C.W.Pike, K.Brew, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.500, 89.700, 45.200, 90.00, 94.50, 90.00
R / Rfree (%)	19.5 / 27

The binding sites of Calcium atom in the Alpha-Lactalbumin (pdb code 1hfy). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Alpha-Lactalbumin, PDB code: 1hfy:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Alpha-Lactalbumin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Alpha-Lactalbumin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca124 b:17.5 occ:1.00 O A:ASP84 2.3 20.3 1.0 O A:LYS79 2.3 14.0 1.0 OD1 A:ASP87 2.4 27.9 1.0 OD1 A:ASP88 2.5 12.5 1.0 OD1 A:ASP82 2.5 34.4 1.0 CG A:ASP87 3.4 22.6 1.0 C A:ASP84 3.5 19.7 1.0 C A:LYS79 3.5 13.6 1.0 CG A:ASP82 3.5 33.0 1.0 OD2 A:ASP87 3.6 21.8 1.0 CG A:ASP88 3.7 12.6 1.0 OD2 A:ASP82 4.0 36.2 1.0 CA A:PHE80 4.1 9.1 1.0 N A:PHE80 4.3 10.4 1.0 OD2 A:ASP88 4.3 15.1 1.0 CA A:ASP84 4.4 22.2 1.0 N A:LEU85 4.4 15.9 1.0 O A:ASP82 4.4 24.6 1.0 CA A:LEU85 4.5 11.7 1.0 N A:ASP84 4.5 25.3 1.0 N A:ASP88 4.5 13.8 1.0 N A:ASP82 4.6 20.1 1.0 CB A:ASP84 4.6 21.8 1.0 C A:PHE80 4.6 11.3 1.0 CA A:LYS79 4.6 17.6 1.0 CB A:ASP87 4.7 17.9 1.0 C A:ASP82 4.7 23.6 1.0 CD1 A:PHE80 4.8 2.0 1.0 CB A:ASP88 4.8 13.1 1.0 CB A:ASP82 4.8 29.3 1.0 N A:ASP87 4.8 14.1 1.0 C A:LEU85 4.8 10.1 1.0 N A:LEU81 4.9 9.7 1.0 CA A:ASP82 4.9 24.1 1.0 CB A:LYS79 5.0 22.4 1.0

Calcium binding site 2 out of 2 in the Alpha-Lactalbumin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Alpha-Lactalbumin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca124 b:18.9 occ:1.00 O B:ASP84 2.2 22.8 1.0 O B:LYS79 2.4 8.9 1.0 OD1 B:ASP87 2.4 14.7 1.0 OD1 B:ASP88 2.5 10.8 1.0 OD1 B:ASP82 2.5 26.3 1.0 CG B:ASP87 3.3 15.5 1.0 C B:ASP84 3.4 22.9 1.0 OD2 B:ASP87 3.4 15.8 1.0 CG B:ASP82 3.5 25.7 1.0 C B:LYS79 3.6 8.1 1.0 CG B:ASP88 3.7 13.0 1.0 OD2 B:ASP82 3.9 32.9 1.0 CA B:PHE80 4.3 9.5 1.0 OD2 B:ASP88 4.3 10.7 1.0 CA B:ASP84 4.4 23.3 1.0 N B:LEU85 4.4 18.6 1.0 N B:PHE80 4.4 7.5 1.0 N B:ASP84 4.4 23.5 1.0 CA B:LEU85 4.4 15.5 1.0 CB B:ASP84 4.5 25.6 1.0 N B:ASP88 4.6 12.4 1.0 O B:ASP82 4.6 16.5 1.0 N B:ASP82 4.6 20.0 1.0 CA B:LYS79 4.7 11.3 1.0 CB B:ASP87 4.7 16.0 1.0 N B:ASP87 4.8 14.0 1.0 C B:PHE80 4.8 12.8 1.0 CB B:ASP82 4.8 22.3 1.0 OD2 B:ASP84 4.8 33.6 1.0 C B:LEU85 4.8 12.1 1.0 C B:ASP82 4.8 19.1 1.0 CB B:ASP88 4.9 6.0 1.0 N B:LEU81 4.9 13.6 1.0 CG B:ASP84 4.9 30.8 1.0 CB B:LYS79 5.0 18.4 1.0 CA B:ASP82 5.0 19.2 1.0 CD1 B:PHE80 5.0 3.0 1.0

A.C.Pike, K.Brew, K.R.Acharya. Crystal Structures of Guinea-Pig, Goat and Bovine Alpha-Lactalbumin Highlight the Enhanced Conformational Flexibility of Regions That Are Significant For Its Action in Lactose Synthase. Structure V. 4 691 1996.
ISSN: ISSN 0969-2126
PubMed: 8805552
DOI: 10.1016/S0969-2126(96)00075-5