Calcium in PDB 2gy7: Angiopoietin-2/TIE2 Complex Crystal Structure

All present enzymatic activity of Angiopoietin-2/TIE2 Complex Crystal Structure:
2.7.10.1;

The structure of Angiopoietin-2/TIE2 Complex Crystal Structure, PDB code: 2gy7 was solved by W.A.Barton, D.B.Nikolov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 3.70
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	165.636, 165.636, 115.310, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 31.7

The binding sites of Calcium atom in the Angiopoietin-2/TIE2 Complex Crystal Structure (pdb code 2gy7). 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 Angiopoietin-2/TIE2 Complex Crystal Structure, PDB code: 2gy7:

Calcium binding site 1 out of 1 in the Angiopoietin-2/TIE2 Complex Crystal Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Angiopoietin-2/TIE2 Complex Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1 b:26.7 occ:1.00 OD2 A:ASP431 1.7 7.5 1.0 OD2 A:ASP429 2.1 9.7 1.0 O A:CYS435 2.6 4.8 1.0 CG A:ASP431 2.7 7.1 1.0 CG A:ASP429 2.8 10.6 1.0 OD1 A:ASP429 2.8 9.4 1.0 OD1 A:ASP431 3.1 6.7 1.0 O A:CYS433 3.4 5.1 1.0 C A:CYS435 3.6 4.9 1.0 CA A:LYS436 4.1 6.3 1.0 CB A:ASP431 4.1 6.5 1.0 O A:ASP431 4.1 3.4 1.0 CB A:ASP429 4.2 10.7 1.0 N A:ASP431 4.2 6.4 1.0 C A:ASP431 4.2 4.2 1.0 N A:LYS436 4.3 5.6 1.0 CG A:LYS436 4.3 8.2 1.0 CA A:ASP431 4.4 5.2 1.0 C A:CYS433 4.4 5.2 1.0 N A:CYS433 4.5 4.6 1.0 N A:CYS435 4.7 5.1 1.0 CB A:LYS436 4.7 7.9 1.0 CA A:ASP429 4.7 9.8 1.0 CA A:CYS435 4.7 4.8 1.0 C A:ASP429 4.7 8.4 1.0 N A:LYS432 4.7 3.4 1.0 CB A:CYS433 4.9 5.0 1.0 CA A:CYS433 4.9 5.0 1.0 N A:ASN430 4.9 7.3 1.0

W.A.Barton, D.Tzvetkova-Robev, E.P.Miranda, M.V.Kolev, K.R.Rajashankar, J.P.Himanen, D.B.Nikolov. Crystal Structures of the TIE2 Receptor Ectodomain and the Angiopoietin-2-TIE2 Complex. Nat.Struct.Mol.Biol. V. 13 524 2006.
ISSN: ISSN 1545-9993
PubMed: 16732286
DOI: 10.1038/NSMB1101