Calcium in PDB 1ezs: Crystal Structure of Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II

All present enzymatic activity of Crystal Structure of Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II:
3.4.21.4;

The structure of Crystal Structure of Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II, PDB code: 1ezs was solved by S.A.Gillmor, T.Takeuchi, S.Q.Yang, C.S.Craik, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	45.828, 59.682, 71.044, 103.57, 93.27, 94.62
R / Rfree (%)	18.8 / 23.5

The binding sites of Calcium atom in the Crystal Structure of Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II (pdb code 1ezs). 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 Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II, PDB code: 1ezs:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II


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 Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca650 b:55.1 occ:1.00 OE1 C:GLU470 2.3 38.2 1.0 OE2 C:GLU480 2.4 55.3 1.0 O C:ASN472 2.5 43.3 1.0 OE1 C:GLU477 2.5 63.8 1.0 O C:VAL475 2.6 45.5 1.0 CD C:GLU470 3.0 31.2 1.0 OE2 C:GLU470 3.1 30.3 1.0 CD C:GLU477 3.5 67.2 1.0 C C:VAL475 3.5 47.0 1.0 C C:ASN472 3.5 39.9 1.0 CD C:GLU480 3.5 53.8 1.0 CG C:GLU477 3.9 64.9 1.0 N C:GLU477 4.0 54.6 1.0 CG C:GLU480 4.1 52.4 1.0 N C:VAL475 4.2 46.1 1.0 N C:LEU476 4.2 47.2 1.0 CA C:LEU476 4.2 48.8 1.0 N C:ASN472 4.3 37.7 1.0 N C:ILE473 4.4 40.7 1.0 CG C:GLU470 4.4 29.8 1.0 CA C:ASN472 4.4 40.1 1.0 CA C:VAL475 4.4 47.6 1.0 CA C:ILE473 4.5 42.0 1.0 OE2 C:GLU477 4.5 69.9 1.0 OE1 C:GLU480 4.5 55.3 1.0 C C:ILE473 4.5 43.8 1.0 CB C:GLU477 4.6 58.7 1.0 CB C:ASN472 4.6 40.3 1.0 C C:LEU476 4.6 51.3 1.0 O C:HOH46 4.7 48.3 1.0 N C:HIS471 4.7 38.3 1.0 O C:ILE473 4.7 44.2 1.0 N C:ASN474 4.8 45.8 1.0 CB C:GLU470 4.8 35.1 1.0 CA C:GLU470 4.9 36.4 1.0 O C:HOH86 4.9 39.1 1.0 CA C:GLU477 4.9 56.9 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II


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 Ecotin Mutant M84R, W67A, G68A, Y69A, D70A Bound to Rat Anionic Trypsin II within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca950 b:33.2 occ:1.00 OE2 D:GLU780 2.4 43.5 1.0 OE1 D:GLU770 2.4 32.6 1.0 O D:ASN772 2.5 33.4 1.0 OE1 D:GLU777 2.5 55.3 1.0 O D:VAL775 2.6 38.0 1.0 OE2 D:GLU770 3.0 25.9 1.0 CD D:GLU770 3.0 22.5 1.0 C D:VAL775 3.5 38.7 1.0 C D:ASN772 3.5 32.5 1.0 CD D:GLU780 3.6 43.4 1.0 CD D:GLU777 3.6 62.3 1.0 CG D:GLU777 4.0 59.5 1.0 N D:VAL775 4.1 36.5 1.0 N D:GLU777 4.1 44.0 1.0 N D:LEU776 4.1 41.0 1.0 CG D:GLU780 4.2 43.4 1.0 CA D:LEU776 4.2 41.0 1.0 CA D:VAL775 4.4 39.8 1.0 N D:ILE773 4.4 31.0 1.0 O D:HOH2 4.4 40.9 1.0 N D:ASN772 4.4 27.9 1.0 CA D:ILE773 4.4 29.9 1.0 C D:ILE773 4.5 30.2 1.0 CA D:ASN772 4.5 28.5 1.0 CG D:GLU770 4.5 25.0 1.0 OE1 D:GLU780 4.6 50.4 1.0 OE2 D:GLU777 4.6 65.0 1.0 CB D:ASN772 4.6 24.3 1.0 O D:ILE773 4.6 32.3 1.0 C D:LEU776 4.7 41.0 1.0 CB D:GLU777 4.7 52.0 1.0 N D:ASN774 4.8 29.3 1.0 O D:HOH42 4.8 35.6 1.0 N D:HIS771 4.8 24.7 1.0 O D:HOH3 4.9 23.6 1.0 CB D:GLU770 5.0 23.3 1.0 CA D:GLU770 5.0 23.5 1.0

S.A.Gillmor, T.Takeuchi, S.Q.Yang, C.S.Craik, R.J.Fletterick. Compromise and Accommodation in Ecotin, A Dimeric Macromolecular Inhibitor of Serine Proteases. J.Mol.Biol. V. 299 993 2000.
ISSN: ISSN 0022-2836
PubMed: 10843853
DOI: 10.1006/JMBI.2000.3812