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Calcium in PDB 2fib: Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Complexed to the Peptide Gly- Pro-Arg-Pro at pH 6.0

Protein crystallography data

The structure of Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Complexed to the Peptide Gly- Pro-Arg-Pro at pH 6.0, PDB code: 2fib 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 / 2.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.330, 68.200, 47.600, 90.00, 105.02, 90.00
R / Rfree (%) 18.6 / 28.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Complexed to the Peptide Gly- Pro-Arg-Pro at pH 6.0 (pdb code 2fib). 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) Complexed to the Peptide Gly- Pro-Arg-Pro at pH 6.0, PDB code: 2fib:

Calcium binding site 1 out of 1 in 2fib

Go back to Calcium Binding Sites List in 2fib
Calcium binding site 1 out of 1 in the Recombinant Human Gamma-Fibrinogen Carboxyl Terminal Fragment (Residues 143-411) Complexed to the Peptide Gly- Pro-Arg-Pro at pH 6.0


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) Complexed to the Peptide Gly- Pro-Arg-Pro at pH 6.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca412

b:31.4
occ:1.00
O A:PHE322 2.2 32.3 1.0
O A:GLY324 2.3 30.3 1.0
OD2 A:ASP318 2.4 27.9 1.0
OD1 A:ASP320 2.4 29.7 1.0
O A:HOH414 2.5 37.8 1.0
O A:HOH413 2.5 17.5 1.0
OD1 A:ASP318 3.0 28.0 1.0
CG A:ASP318 3.0 27.2 1.0
C A:PHE322 3.4 32.3 1.0
CG A:ASP320 3.5 29.9 1.0
C A:GLY324 3.6 30.1 1.0
OD2 A:ASP320 3.8 30.2 1.0
C A:GLU323 4.0 32.4 1.0
N A:GLY324 4.0 31.8 1.0
CA A:GLU323 4.2 32.9 1.0
N A:GLU323 4.3 32.5 1.0
N A:PHE322 4.3 31.5 1.0
O A:HOH422 4.3 50.7 1.0
CA A:PHE322 4.4 32.0 1.0
CA A:ASN325 4.4 28.1 1.0
O A:GLU323 4.4 32.5 1.0
CB A:ASP318 4.4 26.7 1.0
N A:ASN325 4.4 29.2 1.0
CA A:GLY324 4.5 30.9 1.0
O A:ASP320 4.6 28.8 1.0
CB A:PHE322 4.7 32.0 1.0
C A:ASP320 4.7 28.8 1.0
CB A:ASP320 4.8 29.1 1.0
N A:ASP320 4.8 28.1 1.0
CA A:ASP320 5.0 28.6 1.0

Reference:

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
Page generated: Fri Jul 12 10:31:33 2024

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