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Calcium in PDB 1id5: Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin

Enzymatic activity of Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin

All present enzymatic activity of Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin:
3.4.21.5;

Protein crystallography data

The structure of Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin, PDB code: 1id5 was solved by S.X.Wang, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 88.517, 165.377, 83.326, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 26.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin (pdb code 1id5). 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 Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin, PDB code: 1id5:

Calcium binding site 1 out of 1 in 1id5

Go back to Calcium Binding Sites List in 1id5
Calcium binding site 1 out of 1 in the Crystal Structure of Bovine Thrombin Complex with Protease Inhibitor Ecotin


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 Bovine Thrombin Complex with Protease Inhibitor Ecotin within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Ca600

b:64.4
occ:1.00
O H:ARG221A 2.3 24.5 1.0
O H:LYS224 2.4 30.6 1.0
O H:HOH841 2.8 20.6 1.0
O H:HOH840 2.8 33.4 1.0
O H:HOH847 3.1 31.2 1.0
C H:ARG221A 3.3 24.4 1.0
C H:LYS224 3.3 29.6 1.0
N H:ARG221A 3.6 25.2 1.0
N H:LYS224 3.7 32.4 1.0
CA H:LYS224 3.9 31.5 1.0
O H:HOH830 3.9 37.2 1.0
C H:ASP221 4.1 30.9 1.0
CA H:ARG221A 4.1 24.1 1.0
N H:ASP222 4.1 25.2 1.0
O H:TYR184 4.2 28.8 1.0
CB H:LYS224 4.2 32.8 1.0
CA H:ASP222 4.3 26.8 1.0
N H:TYR225 4.3 28.9 1.0
CA H:ASP221 4.4 30.9 1.0
N H:GLY223 4.4 33.7 1.0
C H:ASP222 4.5 26.1 1.0
CA H:TYR225 4.6 27.6 1.0
O H:HOH822 4.7 17.0 1.0
O H:ASP221 4.7 32.7 1.0
OD1 H:ASP221 4.8 33.1 1.0
C H:GLY223 4.8 35.1 1.0
CB H:ARG221A 5.0 21.8 1.0
CD1 H:TYR225 5.0 25.4 1.0

Reference:

S.X.Wang, C.T.Esmon, R.J.Fletterick. Crystal Structure of Thrombin-Ecotin Reveals Conformational Changes and Extended Interactions. Biochemistry V. 40 10038 2001.
ISSN: ISSN 0006-2960
PubMed: 11513582
DOI: 10.1021/BI010712H
Page generated: Mon Jul 7 15:49:15 2025

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