Calcium in PDB 1fkv: Recombinant Goat Alpha-Lactalbumin T29I

All present enzymatic activity of Recombinant Goat Alpha-Lactalbumin T29I:
2.4.1.22;

The structure of Recombinant Goat Alpha-Lactalbumin T29I, PDB code: 1fkv was solved by K.Horii, M.Matsushima, K.Tsumoto, I.Kumagai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	44.800, 88.740, 32.380, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 29.2

The binding sites of Calcium atom in the Recombinant Goat Alpha-Lactalbumin T29I (pdb code 1fkv). 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 Recombinant Goat Alpha-Lactalbumin T29I, PDB code: 1fkv:

Calcium binding site 1 out of 1 in the Recombinant Goat Alpha-Lactalbumin T29I


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Recombinant Goat Alpha-Lactalbumin T29I within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca124 b:13.3 occ:1.00 O A:ASP84 2.3 10.4 1.0 OD2 A:ASP88 2.4 11.4 1.0 OD2 A:ASP82 2.5 20.2 1.0 OD1 A:ASP87 2.5 14.1 1.0 O A:LYS79 2.6 12.3 1.0 O A:HOH143 2.6 8.5 1.0 O A:HOH132 2.8 16.7 1.0 C A:ASP84 3.4 13.3 1.0 CG A:ASP82 3.4 18.7 1.0 CG A:ASP87 3.5 12.5 1.0 CG A:ASP88 3.6 12.6 1.0 C A:LYS79 3.7 12.4 1.0 OD2 A:ASP87 3.7 11.2 1.0 OD1 A:ASP82 3.8 20.4 1.0 CA A:PHE80 4.1 11.1 1.0 OD1 A:ASP88 4.2 12.1 1.0 CA A:ASP84 4.3 18.0 1.0 N A:LEU85 4.3 11.8 1.0 O A:ASP82 4.3 15.1 1.0 CA A:LEU85 4.3 11.3 1.0 N A:ASP84 4.4 19.2 1.0 N A:PHE80 4.4 12.2 1.0 N A:ASP88 4.4 11.1 1.0 CB A:ASP84 4.5 23.5 1.0 N A:ASP82 4.5 18.2 1.0 OD2 A:ASP84 4.6 32.7 1.0 C A:PHE80 4.7 13.2 1.0 C A:ASP82 4.7 17.7 1.0 CB A:ASP88 4.7 12.9 1.0 CB A:ASP82 4.7 18.6 1.0 C A:LEU85 4.8 10.7 1.0 N A:ASP87 4.8 8.7 1.0 CD2 A:PHE80 4.8 8.9 1.0 CA A:LYS79 4.8 13.4 1.0 CB A:ASP87 4.8 9.9 1.0 N A:LEU81 4.9 13.1 1.0 CA A:ASP82 4.9 17.3 1.0 CG A:ASP84 4.9 26.1 1.0 N A:THR86 5.0 11.6 1.0

K.Horii, M.Saito, T.Yoda, K.Tsumoto, M.Matsushima, K.Kuwajima, I.Kumagai. Contribution of THR29 to the Thermodynamic Stability of Goat Alpha-Lactalbumin As Determined By Experimental and Theoretical Approaches. Proteins V. 45 16 2001.
ISSN: ISSN 0887-3585
PubMed: 11536356
DOI: 10.1002/PROT.1119