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Calcium in PDB 6bfp: Bovine Trypsin Bound to Potent Inhibitor

Enzymatic activity of Bovine Trypsin Bound to Potent Inhibitor

All present enzymatic activity of Bovine Trypsin Bound to Potent Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of Bovine Trypsin Bound to Potent Inhibitor, PDB code: 6bfp was solved by J.R.Partridge, R.M.Choy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.41 / 1.29
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.510, 58.330, 66.580, 90.00, 90.00, 90.00
R / Rfree (%) 12.9 / 14.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Bovine Trypsin Bound to Potent Inhibitor (pdb code 6bfp). 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 Bovine Trypsin Bound to Potent Inhibitor, PDB code: 6bfp:

Calcium binding site 1 out of 1 in 6bfp

Go back to Calcium Binding Sites List in 6bfp
Calcium binding site 1 out of 1 in the Bovine Trypsin Bound to Potent Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bovine Trypsin Bound to Potent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:6.1
occ:1.00
O A:VAL80 2.3 6.8 1.0
OE1 A:GLU75 2.3 6.5 1.0
OE2 A:GLU85 2.3 7.0 1.0
O A:ASN77 2.3 6.3 1.0
O A:HOH509 2.3 7.4 1.0
O A:HOH417 2.4 6.8 1.0
HA A:VAL81 3.3 8.7 1.0
HG2 A:GLU85 3.4 10.2 1.0
CD A:GLU75 3.4 5.8 1.0
CD A:GLU85 3.4 6.8 1.0
C A:VAL80 3.4 7.1 1.0
C A:ASN77 3.5 6.1 1.0
H A:GLU82 3.5 9.0 1.0
HA A:ILE78 3.5 6.7 1.0
H A:VAL80 3.6 8.3 1.0
HG3 A:GLU82 3.7 10.6 1.0
CG A:GLU85 3.7 8.5 1.0
HG3 A:GLU85 3.7 10.2 1.0
OE2 A:GLU75 3.8 6.3 1.0
H A:ASP76 3.8 7.2 1.0
HA A:GLU75 3.9 6.2 1.0
CA A:VAL81 4.1 7.3 1.0
N A:GLU82 4.2 7.5 1.0
N A:VAL81 4.2 7.3 1.0
HB3 A:ASN77 4.2 9.1 1.0
N A:VAL80 4.2 6.9 1.0
CA A:ILE78 4.2 5.6 1.0
HB2 A:GLU82 4.3 9.9 1.0
OE1 A:GLU82 4.3 7.7 1.0
N A:ILE78 4.3 5.7 1.0
H A:ASN77 4.3 7.6 1.0
N A:ASN77 4.4 6.3 1.0
CA A:VAL80 4.4 7.3 1.0
CA A:ASN77 4.4 6.1 1.0
O A:HOH532 4.5 7.5 1.0
OE1 A:GLU85 4.5 7.5 1.0
CG A:GLU82 4.5 8.8 1.0
C A:ILE78 4.5 5.9 1.0
HB3 A:GLU75 4.5 6.7 1.0
N A:ASP76 4.6 6.0 1.0
HB A:VAL80 4.6 9.1 1.0
CG A:GLU75 4.6 6.1 1.0
C A:VAL81 4.7 7.5 1.0
CA A:GLU75 4.7 5.2 1.0
HG21 A:VAL81 4.8 10.4 1.0
CB A:GLU82 4.8 8.3 1.0
CD A:GLU82 4.8 9.9 1.0
CB A:ASN77 4.8 7.6 1.0
CB A:GLU75 4.8 5.6 1.0
N A:ASN79 4.9 6.3 1.0
O A:ILE78 4.9 6.0 1.0
HZ A:PHE87 4.9 13.9 1.0
H A:ASN79 4.9 7.5 1.0
C A:ASP76 5.0 6.3 1.0

Reference:

J.R.Partridge, R.M.Choy, A.Silva-Garcia, C.Yu, Z.Li, H.Sham, B.Metcalf. Structures of Full-Length Plasma Kallikrein Bound to Highly Specific Inhibitors Describe A New Mode of Targeted Inhibition. J.Struct.Biol. V. 206 170 2019.
ISSN: ESSN 1095-8657
PubMed: 30876891
DOI: 10.1016/J.JSB.2019.03.001
Page generated: Wed Jul 9 12:46:59 2025

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