Calcium in PDB 3fib: Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Bound to Calcium at pH 6.0: A Further Refinement of Pdb Entry 1FIB, and Differs From 1FIB By the Modelling of A Cis Peptide Bond Between Residues K338 and C339

The structure of Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Bound to Calcium at pH 6.0: A Further Refinement of Pdb Entry 1FIB, and Differs From 1FIB By the Modelling of A Cis Peptide Bond Between Residues K338 and C339, PDB code: 3fib was solved by K.P.Pratt, H.C.F.Cote, D.W.Chung, R.E.Stenkamp, E.W.Davie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.530, 68.420, 47.670, 90.00, 105.36, 90.00
R / Rfree (%)	15.4 / 20.6

The binding sites of Calcium atom in the Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Bound to Calcium at pH 6.0: A Further Refinement of Pdb Entry 1FIB, and Differs From 1FIB By the Modelling of A Cis Peptide Bond Between Residues K338 and C339 (pdb code 3fib). 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 Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Bound to Calcium at pH 6.0: A Further Refinement of Pdb Entry 1FIB, and Differs From 1FIB By the Modelling of A Cis Peptide Bond Between Residues K338 and C339, PDB code: 3fib:

Calcium binding site 1 out of 1 in the Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Bound to Calcium at pH 6.0: A Further Refinement of Pdb Entry 1FIB, and Differs From 1FIB By the Modelling of A Cis Peptide Bond Between Residues K338 and C339


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Bound to Calcium at pH 6.0: A Further Refinement of Pdb Entry 1FIB, and Differs From 1FIB By the Modelling of A Cis Peptide Bond Between Residues K338 and C339 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca400 b:14.6 occ:1.00 O A:PHE322 2.3 10.5 1.0 O A:GLY324 2.4 15.6 1.0 O A:HOH401 2.4 10.1 1.0 O A:HOH402 2.4 14.8 1.0 OD2 A:ASP318 2.5 13.6 1.0 OD1 A:ASP320 2.5 13.3 1.0 OD1 A:ASP318 2.8 14.3 1.0 CG A:ASP318 3.0 12.1 1.0 CG A:ASP320 3.5 12.1 1.0 C A:PHE322 3.5 13.8 1.0 C A:GLY324 3.6 14.5 1.0 OD2 A:ASP320 3.8 13.2 1.0 N A:PHE322 4.2 13.4 1.0 CA A:PHE322 4.2 12.5 1.0 C A:GLU323 4.3 17.6 1.0 O A:HOH417 4.3 34.5 1.0 O A:GLU323 4.3 17.3 1.0 O A:ASP320 4.4 11.2 1.0 N A:GLY324 4.4 16.8 1.0 CB A:ASP318 4.4 10.9 1.0 CB A:PHE322 4.4 10.9 1.0 CA A:ASN325 4.4 11.1 1.0 N A:GLU323 4.5 15.4 1.0 N A:ASN325 4.5 11.4 1.0 CA A:GLY324 4.6 15.0 1.0 C A:ASP320 4.7 10.2 1.0 CA A:GLU323 4.7 18.8 1.0 N A:ASP320 4.8 6.7 1.0 CB A:ASP320 4.8 9.5 1.0 CA A:ASP320 5.0 8.3 1.0

K.P.Pratt, H.C.Cote, D.W.Chung, R.E.Stenkamp, E.W.Davie. The Primary Fibrin Polymerization Pocket: Three-Dimensional Structure of A 30-kDa C-Terminal Gamma Chain Fragment Complexed with the Peptide Gly-Pro-Arg-Pro. Proc.Natl.Acad.Sci.Usa V. 94 7176 1997.
ISSN: ISSN 0027-8424
PubMed: 9207064
DOI: 10.1073/PNAS.94.14.7176