Calcium in PDB 8epc: Crystal Structure of Human Coagulation Factor Ixa (S195A), Apo-Form

The structure of Crystal Structure of Human Coagulation Factor Ixa (S195A), Apo-Form, PDB code: 8epc was solved by V.N.Kolyadko, S.Krishnaswamy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.87 / 2.51
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	67.975, 67.975, 109.82, 90, 90, 120
R / Rfree (%)	23.1 / 28.1

The binding sites of Calcium atom in the Crystal Structure of Human Coagulation Factor Ixa (S195A), Apo-Form (pdb code 8epc). 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 Human Coagulation Factor Ixa (S195A), Apo-Form, PDB code: 8epc:

Calcium binding site 1 out of 1 in the Crystal Structure of Human Coagulation Factor Ixa (S195A), Apo-Form


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 Human Coagulation Factor Ixa (S195A), Apo-Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:104.5 occ:1.00 O B:GLU75 2.2 105.3 1.0 OE2 B:GLU80 2.3 94.7 1.0 O B:ASN72 2.4 98.3 1.0 OE1 B:GLU70 2.5 88.1 1.0 OE1 B:GLU77 2.6 96.0 1.0 CD B:GLU80 3.3 90.7 1.0 CD B:GLU70 3.3 85.9 1.0 OE2 B:GLU70 3.4 88.1 1.0 C B:GLU75 3.4 109.3 1.0 C B:ASN72 3.5 98.4 1.0 CD B:GLU77 3.6 98.5 1.0 CG B:GLU80 3.6 86.4 1.0 CA B:ILE73 4.0 99.3 1.0 OE2 B:GLU77 4.0 99.1 1.0 N B:ILE73 4.2 98.8 1.0 C B:ILE73 4.2 105.2 1.0 N B:GLU75 4.2 113.3 1.0 N B:THR76 4.3 111.5 1.0 CA B:THR76 4.4 108.1 1.0 O B:ILE73 4.4 106.1 1.0 CA B:GLU75 4.4 114.5 1.0 OE1 B:GLU80 4.4 90.9 1.0 N B:GLU77 4.5 102.5 1.0 N B:ASN72 4.5 93.1 1.0 CA B:ASN72 4.6 97.9 1.0 N B:GLU74 4.8 109.7 1.0 CG B:GLU70 4.8 82.2 1.0 CG B:GLU77 4.8 101.2 1.0 N B:HIS71 4.9 82.8 1.0

V.N.Kolyadko, J.M.Layzer, K.Perry, B.A.Sullenger, S.Krishnaswamy. Allosteric Control of Coagulation Factor Ixa Via Its Exosite II Regulates Blood Clotting Proc.Natl.Acad.Sci.Usa 2024.
ISSN: ESSN 1091-6490
DOI: 10.1073/PNAS.2401136121