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Calcium in PDB 3fp6: Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit

Enzymatic activity of Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit

All present enzymatic activity of Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit:
3.4.21.4;

Protein crystallography data

The structure of Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit, PDB code: 3fp6 was solved by E.Zakharova, M.P.Horvath, D.P.Goldenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.49
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.634, 91.634, 61.352, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 20.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit (pdb code 3fp6). 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 Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit, PDB code: 3fp6:

Calcium binding site 1 out of 1 in 3fp6

Go back to Calcium Binding Sites List in 3fp6
Calcium binding site 1 out of 1 in the Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Anionic Trypsin in Complex with Bovine Pancreatic Trypsin Inhibitor (Bpti) Determined to the 1.49 A Resolution Limit within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca601

b:11.0
occ:1.00
 OE1 E:GLU70 2.2 10.6 1.0
O E:VAL75 2.3 10.2 1.0
O E:HOH776 2.3 14.3 1.0
OE2 E:GLU80 2.3 10.9 1.0
O E:ASN72 2.3 11.1 1.0
OE1 E:GLU77 2.5 17.9 1.0
CD E:GLU77 3.3 20.6 1.0
CD E:GLU70 3.3 10.2 1.0
CD E:GLU80 3.3 10.7 1.0
C E:ASN72 3.4 10.6 1.0
C E:VAL75 3.5 10.3 1.0
CG E:GLU77 3.6 19.7 1.0
CG E:GLU80 3.7 12.2 1.0
OE2 E:GLU70 3.7 10.4 1.0
N E:GLU77 4.0 14.4 1.0
N E:ASN72 4.3 11.2 1.0
N E:VAL75 4.3 9.2 1.0
CA E:ILE73 4.3 10.2 1.0
N E:ILE73 4.3 10.5 1.0
OE2 E:GLU77 4.3 19.6 1.0
CA E:LEU76 4.3 10.7 1.0
N E:LEU76 4.3 9.8 1.0
O E:HOH887 4.3 22.2 1.0
CB E:GLU77 4.3 17.9 1.0
CA E:ASN72 4.4 10.8 1.0
CA E:VAL75 4.4 10.2 1.0
OE1 E:GLU80 4.5 12.4 1.0
C E:ILE73 4.5 10.4 1.0
CG E:GLU70 4.6 9.7 1.0
CB E:ASN72 4.6 11.3 1.0
N E:HIS71 4.7 10.3 1.0
C E:LEU76 4.7 13.3 1.0
CA E:GLU70 4.8 10.0 1.0
CA E:GLU77 4.9 18.0 1.0
O E:ILE73 4.9 10.2 1.0
CB E:GLU70 4.9 8.9 1.0
N E:ASN74 4.9 8.9 1.0

Reference:

E.Zakharova, M.P.Horvath, D.P.Goldenberg. Structure of A Serine Protease Poised to Resynthesize A Peptide Bond. Proc.Natl.Acad.Sci.Usa V. 106 11034 2009.
ISSN: ISSN 0027-8424
PubMed: 19549826
DOI: 10.1073/PNAS.0902463106
Page generated: Tue Jul 8 12:28:17 2025

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