Calcium in PDB 1h30: C-Terminal Lg Domain Pair of Human GAS6

The structure of C-Terminal Lg Domain Pair of Human GAS6, PDB code: 1h30 was solved by T.Sasaki, P.G.Knyazev, Y.Cheburkin, W.Gohring, D.Tisi, A.Ullrich, R.Timpl, E.Hohenester, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20 / 2.2
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	111.310, 111.310, 217.720, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 25.9

The binding sites of Calcium atom in the C-Terminal Lg Domain Pair of Human GAS6 (pdb code 1h30). 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 C-Terminal Lg Domain Pair of Human GAS6, PDB code: 1h30:

Calcium binding site 1 out of 1 in the C-Terminal Lg Domain Pair of Human GAS6


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of C-Terminal Lg Domain Pair of Human GAS6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca701 b:26.5 occ:1.00 O A:ARG440 2.4 19.3 1.0 OD2 A:ASP656 2.5 22.8 1.0 O A:HOH2102 2.6 20.1 1.0 O A:GLU331 2.6 25.6 1.0 OD2 A:ASP329 2.6 19.6 1.0 O A:HOH2040 2.7 24.7 1.0 OD1 A:ASP329 2.7 19.8 1.0 CG A:ASP329 3.0 24.0 1.0 CG A:ASP656 3.5 25.2 1.0 C A:GLU331 3.6 22.2 1.0 C A:ARG440 3.6 22.2 1.0 NE2 A:HIS668 4.0 23.2 1.0 CB A:ASP656 4.0 18.5 1.0 CD2 A:HIS668 4.2 21.2 1.0 N A:GLU331 4.3 22.4 1.0 CA A:GLU331 4.3 23.0 1.0 O A:HOH2108 4.3 25.1 1.0 CA A:LEU441 4.4 23.8 1.0 CB A:GLU331 4.4 23.6 1.0 N A:LEU441 4.4 20.8 1.0 OD1 A:ASP656 4.5 22.6 1.0 CB A:ASP329 4.5 19.9 1.0 O A:ASN438 4.6 30.3 1.0 N A:GLY332 4.6 21.4 1.0 CA A:ARG440 4.6 21.4 1.0 CB A:ARG440 4.6 22.9 1.0 CA A:GLY332 4.7 20.1 1.0 OD2 A:ASP654 4.8 35.2 1.0 N A:ASP442 4.9 22.1 1.0

T.Sasaki, P.G.Knyazev, Y.Cheburkin, W.Gohring, D.Tisi, A.Ullrich, R.Timpl, E.Hohenester. Crystal Structure of A Carboxy-Terminal Fragment of Growth-Arrest-Specific Protein GAS6: Receptor Tyrosine Kinase Activation By Laminin G-Like Domains J.Biol.Chem. V. 277 44164 2002.
ISSN: ISSN 0021-9258
PubMed: 12218057
DOI: 10.1074/JBC.M207340200