Calcium in PDB 1klj: Crystal Structure of Uninhibited Factor Viia

All present enzymatic activity of Crystal Structure of Uninhibited Factor Viia:
3.4.21.21;

The structure of Crystal Structure of Uninhibited Factor Viia, PDB code: 1klj was solved by K.Sichler, D.Banner, A.D'arcy, K.P.Hopfner, R.Huber, W.Bode, G.B.Kresse, E.Kopetzki, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.44
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.443, 94.443, 114.315, 90.00, 90.00, 90.00
R / Rfree (%)	23.1 / 28.6

The binding sites of Calcium atom in the Crystal Structure of Uninhibited Factor Viia (pdb code 1klj). 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 Crystal Structure of Uninhibited Factor Viia, PDB code: 1klj:

Calcium binding site 1 out of 1 in the Crystal Structure of Uninhibited Factor Viia


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Uninhibited Factor Viia within 5.0Å range: probe atom residue distance (Å) B Occ H:Ca900 b:45.1 occ:1.00 O H:GLU75 2.3 47.3 1.0 OE1 H:GLU80 2.3 30.4 1.0 O H:HOH812 2.3 39.7 1.0 OE1 H:GLU70 2.5 49.0 1.0 O H:ASP72 2.5 35.4 1.0 CD H:GLU70 3.2 47.4 1.0 OE2 H:GLU70 3.2 47.2 1.0 CD H:GLU80 3.3 33.7 1.0 C H:GLU75 3.5 48.0 1.0 CG H:GLU80 3.5 34.2 1.0 C H:ASP72 3.6 38.1 1.0 O H:HOH809 3.7 39.4 1.0 CA H:HIS76 4.1 45.6 1.0 N H:HIS76 4.3 46.1 1.0 N H:GLU75 4.3 48.5 1.0 N H:ASP72 4.4 38.6 1.0 CA H:GLU75 4.4 49.0 1.0 OE2 H:GLU80 4.5 35.9 1.0 N H:LEU73 4.5 39.2 1.0 CA H:LEU73 4.5 40.7 1.0 CA H:ASP72 4.6 39.5 1.0 CG H:GLU70 4.7 45.8 1.0 N H:HIS71 4.7 38.3 1.0 N H:ASP77 4.7 43.2 1.0 C H:LEU73 4.8 41.7 1.0 CB H:ASP72 4.9 42.6 1.0 C H:HIS76 4.9 45.1 1.0 CB H:GLU80 5.0 35.3 1.0

K.Sichler, D.W.Banner, A.D'arcy, K.P.Hopfner, R.Huber, W.Bode, G.B.Kresse, E.Kopetzki, H.Brandstetter. Crystal Structures of Uninhibited Factor Viia Link Its Cofactor and Substrate-Assisted Activation to Specific Interactions. J.Mol.Biol. V. 322 591 2002.
ISSN: ISSN 0022-2836
PubMed: 12225752
DOI: 10.1016/S0022-2836(02)00747-7