Calcium in PDB 1fzb: Crystal Structure of Crosslinked Fragment D

The structure of Crystal Structure of Crosslinked Fragment D, PDB code: 1fzb was solved by G.Spraggon, S.J.Everse, R.F.Doolittle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.820, 95.500, 113.760, 90.00, 96.08, 90.00
R / Rfree (%)	24.1 / 31.8

The binding sites of Calcium atom in the Crystal Structure of Crosslinked Fragment D (pdb code 1fzb). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Crosslinked Fragment D, PDB code: 1fzb:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Crosslinked Fragment D


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 Crosslinked Fragment D within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1 b:43.3 occ:1.00 O C:PHE322 2.4 43.5 1.0 OD1 C:ASP320 2.5 46.4 1.0 OD1 C:ASP318 2.6 52.5 1.0 CG C:ASP318 3.1 58.6 1.0 N C:ASN325 3.4 40.0 1.0 OD2 C:ASP318 3.5 64.8 1.0 C C:PHE322 3.5 41.7 1.0 N C:GLY324 3.6 49.1 1.0 CG C:ASP320 3.7 47.0 1.0 O C:ASP320 3.9 44.7 1.0 C C:GLU323 4.1 51.6 1.0 CA C:GLU323 4.1 52.3 1.0 CA C:ASN325 4.1 41.1 1.0 CB C:ASP318 4.1 54.1 1.0 OD2 C:ASP320 4.2 48.4 1.0 N C:GLU323 4.2 47.5 1.0 C C:GLY324 4.3 46.4 1.0 CA C:GLY324 4.3 46.6 1.0 C C:ASP320 4.6 43.8 1.0 CA C:PHE322 4.6 38.0 1.0 N C:ASP320 4.7 47.8 1.0 N C:PHE322 4.7 41.2 1.0 CB C:ASN325 4.8 36.8 1.0 CB C:ASP320 4.9 46.2 1.0 CB C:PHE322 4.9 38.3 1.0 CA C:ASP320 4.9 46.0 1.0 O C:GLU323 4.9 50.5 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Crosslinked Fragment D


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Crosslinked Fragment D within 5.0Å range: probe atom residue distance (Å) B Occ F:Ca1 b:28.4 occ:1.00 O F:PHE322 2.3 43.7 1.0 OD1 F:ASP320 2.4 40.3 1.0 OD1 F:ASP318 2.7 50.0 1.0 N F:ASN325 3.2 42.4 1.0 CG F:ASP318 3.3 56.3 1.0 N F:GLY324 3.4 45.8 1.0 C F:PHE322 3.4 39.2 1.0 CG F:ASP320 3.5 43.9 1.0 OD2 F:ASP318 3.6 63.6 1.0 O F:ASP320 3.8 37.1 1.0 C F:GLU323 3.9 46.2 1.0 OD2 F:ASP320 4.0 46.2 1.0 CA F:ASN325 4.0 39.9 1.0 CA F:GLU323 4.0 48.9 1.0 CA F:GLY324 4.1 44.4 1.0 C F:GLY324 4.1 48.0 1.0 N F:GLU323 4.1 42.6 1.0 CB F:ASP318 4.3 51.4 1.0 CA F:PHE322 4.4 38.0 1.0 C F:ASP320 4.5 42.5 1.0 N F:PHE322 4.5 41.3 1.0 CB F:PHE322 4.6 38.5 1.0 CB F:ASN325 4.7 38.9 1.0 N F:ASP320 4.7 44.9 1.0 CB F:ASP320 4.8 39.9 1.0 O F:GLU323 4.8 45.4 1.0 CA F:ASP320 4.9 42.5 1.0

G.Spraggon, S.J.Everse, R.F.Doolittle. Crystal Structures of Fragment D From Human Fibrinogen and Its Crosslinked Counterpart From Fibrin. Nature V. 389 455 1997.
ISSN: ISSN 0028-0836
PubMed: 9333233
DOI: 10.1038/38947