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Calcium in PDB 6zr3: Crystal Structure of Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound

Protein crystallography data

The structure of Crystal Structure of Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound, PDB code: 6zr3 was solved by A.K.Shrive, T.J.Greenhough, H.M.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.28 / 1.97
Space group P 4
Cell size a, b, c (Å), α, β, γ (°) 119.019, 119.019, 44.31, 90, 90, 90
R / Rfree (%) 18.4 / 22.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound (pdb code 6zr3). 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 Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound, PDB code: 6zr3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6zr3

Go back to Calcium Binding Sites List in 6zr3
Calcium binding site 1 out of 2 in the Crystal Structure of Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound


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 Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:40.8
occ:1.00
OD1 A:ASP395 2.3 40.5 1.0
O A:ASN399 2.4 46.0 1.0
OD2 A:ASP393 2.4 39.6 1.0
O A:HOH652 2.5 38.2 1.0
O A:SER397 2.6 54.6 1.0
OD1 A:ASP393 2.6 35.1 1.0
O A:HOH639 2.6 40.3 1.0
CG A:ASP393 2.8 37.6 1.0
CG A:ASP395 3.2 42.8 1.0
OD2 A:ASP395 3.4 41.5 1.0
C A:ASN399 3.5 47.6 1.0
C A:SER397 3.5 53.6 1.0
O A:ASP395 4.2 41.1 1.0
C A:GLU398 4.2 55.3 1.0
N A:SER397 4.2 52.2 1.0
N A:ASN399 4.3 54.8 1.0
N A:ASN400 4.3 41.1 1.0
CA A:SER397 4.3 53.1 1.0
CB A:ASP393 4.3 37.5 1.0
N A:GLU398 4.4 54.6 1.0
CA A:ASN400 4.4 39.4 1.0
C A:ASP395 4.4 45.4 1.0
CA A:GLU398 4.5 57.5 1.0
O A:HOH611 4.5 48.0 1.0
CB A:ASP395 4.5 43.0 1.0
N A:ASP395 4.5 41.6 1.0
CB A:SER397 4.5 51.9 1.0
CA A:ASN399 4.5 52.0 1.0
O A:GLU398 4.6 52.6 1.0
CA A:ASP395 4.7 42.8 1.0
OG A:SER397 4.9 51.0 1.0
N A:HIS396 5.0 49.3 1.0

Calcium binding site 2 out of 2 in 6zr3

Go back to Calcium Binding Sites List in 6zr3
Calcium binding site 2 out of 2 in the Crystal Structure of Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound


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 Tetrameric Fibrinogen-Like Recognition Domain of FIBCD1 with N-Acetyl-Galactosamine-4-Sulfate Ligand Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca501

b:36.6
occ:1.00
O B:HOH688 2.3 37.8 1.0
O B:ASN399 2.3 36.9 1.0
OD1 B:ASP395 2.4 35.6 1.0
O B:HOH643 2.4 34.3 1.0
O B:SER397 2.4 41.1 1.0
OD2 B:ASP393 2.5 36.8 1.0
OD1 B:ASP393 2.6 34.1 1.0
CG B:ASP393 2.8 38.1 1.0
CG B:ASP395 3.3 37.0 1.0
C B:SER397 3.5 45.0 1.0
C B:ASN399 3.5 40.6 1.0
OD2 B:ASP395 3.7 36.4 1.0
O B:ASP395 4.1 33.6 1.0
N B:SER397 4.1 42.1 1.0
CA B:SER397 4.2 43.2 1.0
C B:GLU398 4.2 49.7 1.0
N B:ASN399 4.3 48.2 1.0
N B:ASN400 4.3 35.9 1.0
CB B:ASP393 4.3 38.5 1.0
O B:GLU398 4.3 52.2 1.0
CB B:SER397 4.3 42.9 1.0
C B:ASP395 4.4 36.7 1.0
CA B:ASN400 4.5 32.6 1.0
N B:GLU398 4.5 47.2 1.0
CA B:ASN399 4.5 44.2 1.0
CB B:ASP395 4.6 35.6 1.0
N B:ASP395 4.6 35.1 1.0
CA B:GLU398 4.7 51.4 1.0
CA B:ASP395 4.8 35.9 1.0
OG B:SER397 4.9 42.0 1.0

Reference:

H.M.Williams, J.B.Moeller, I.Burns, A.Schlosser, G.L.Sorensen, T.J.Greenhough, U.Holmskov, A.K.Shrive. Crystal Structures of Human Immune Protein FIBCD1 Reveal An Extended Ligand Binding Site Compatible with Recognition of Chitin Oligomers To Be Published.
Page generated: Wed Jul 9 20:37:01 2025

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