Calcium in PDB 1ex0: Human Factor XIII, Mutant W279F Zymogen

All present enzymatic activity of Human Factor XIII, Mutant W279F Zymogen:
2.3.2.13;

The structure of Human Factor XIII, Mutant W279F Zymogen, PDB code: 1ex0 was solved by R.J.Garzon, K.P.Pratt, P.D.Bishop, I.Le Trong, R.E.Stenkamp, D.C.Teller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.94 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	100.540, 70.640, 133.380, 90.00, 106.08, 90.00
R / Rfree (%)	18.7 / 23.4

The binding sites of Calcium atom in the Human Factor XIII, Mutant W279F Zymogen (pdb code 1ex0). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Human Factor XIII, Mutant W279F Zymogen, PDB code: 1ex0:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Human Factor XIII, Mutant W279F Zymogen


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human Factor XIII, Mutant W279F Zymogen within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1320 b:30.1 occ:1.00 O A:HOH1646 2.8 41.6 1.0 O A:HOH1518 2.8 33.7 1.0 O A:ALA457 2.8 29.7 1.0 O A:ASN436 2.8 23.9 1.0 OD1 A:ASP438 2.9 22.4 1.0 O A:HOH1408 3.1 26.6 1.0 O A:HOH1824 3.4 58.2 1.0 C A:ASN436 3.6 21.9 1.0 O A:SER437 3.7 20.0 1.0 C A:ALA457 3.8 29.9 1.0 CA A:ALA457 4.0 29.0 1.0 CB A:ALA457 4.0 29.3 1.0 C A:SER437 4.0 19.0 1.0 CG A:ASP438 4.1 22.2 1.0 O A:HOH1428 4.1 27.5 1.0 CA A:ASN436 4.2 21.6 1.0 O A:HOH1620 4.3 39.5 1.0 N A:ASP438 4.3 19.6 1.0 N A:SER437 4.5 18.0 1.0 O A:HOH1383 4.6 24.8 1.0 CA A:SER437 4.7 19.5 1.0 CA A:ASP438 4.7 21.3 1.0 CB A:ASN436 4.8 23.2 1.0 O A:HOH1754 4.8 49.6 1.0 OE2 A:GLU490 4.9 42.7 1.0 OD2 A:ASP438 4.9 23.2 1.0 N A:THR458 5.0 26.8 1.0

Calcium binding site 2 out of 2 in the Human Factor XIII, Mutant W279F Zymogen


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Human Factor XIII, Mutant W279F Zymogen within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1321 b:21.6 occ:1.00 OD1 B:ASP438 2.7 26.2 1.0 O B:HOH1692 2.8 35.1 1.0 O B:ALA457 2.8 25.7 1.0 O B:HOH1536 2.9 27.9 1.0 O B:ASN436 2.9 20.8 1.0 O B:HOH1417 3.0 20.8 1.0 O B:SER437 3.6 16.8 1.0 C B:ASN436 3.7 21.2 1.0 C B:ALA457 3.8 24.0 1.0 CB B:ALA457 3.9 26.1 1.0 O B:HOH1608 3.9 31.4 1.0 CA B:ALA457 3.9 24.9 1.0 CG B:ASP438 4.0 26.2 1.0 C B:SER437 4.0 19.5 1.0 O B:HOH1439 4.1 22.4 1.0 CA B:ASN436 4.3 19.4 1.0 N B:ASP438 4.4 20.1 1.0 O B:HOH1513 4.4 26.7 1.0 N B:SER437 4.5 19.8 1.0 CA B:ASP438 4.6 24.0 1.0 OE2 B:GLU490 4.6 35.3 1.0 O B:HOH1373 4.6 17.4 1.0 O B:HOH1840 4.7 42.7 1.0 OD2 B:ASP438 4.7 25.5 1.0 CA B:SER437 4.8 20.6 1.0 CB B:ASN436 4.9 19.3 1.0 CB B:ASP438 4.9 24.9 1.0 N B:THR458 5.0 22.4 1.0

R.J.Garzon, K.P.Pratt, P.D.Bishop, I.Le Trong, R.E.Stenkamp, D.C.Teller. Tryptophan 279 Is Essential For the Transglutaminase Activity of Coagulation Factor XIII: Functional and Structural Characterization To Be Published.