Calcium in PDB 1hle: Crystal Structure of Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 Angstroms Resolution

The structure of Crystal Structure of Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 Angstroms Resolution, PDB code: 1hle was solved by U.Baumann, W.Bode, R.Huber, J.Travis, J.Potempa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.95
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.370, 103.570, 80.930, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / n/a

The binding sites of Calcium atom in the Crystal Structure of Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 Angstroms Resolution (pdb code 1hle). 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 Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 Angstroms Resolution, PDB code: 1hle:

Calcium binding site 1 out of 1 in the Crystal Structure of Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 Angstroms Resolution


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 Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca647 b:14.8 occ:0.50 OE1 A:GLU166 2.5 28.7 1.0 OE2 A:GLU166 2.8 28.4 1.0 CD A:GLU166 3.0 25.5 1.0 H1 A:HOH718 3.5 0.0 0.5 HZ1 A:LYS113 4.2 0.0 1.0 O A:HOH718 4.4 17.8 0.5 H2 A:HOH718 4.4 0.0 0.5 O A:GLY163 4.4 20.3 1.0 O A:HOH717 4.5 54.1 1.0 CG A:GLU166 4.6 21.3 1.0 H2 A:HOH717 4.6 0.0 1.0 H1 A:HOH717 4.7 0.0 1.0 O A:HOH683 4.9 42.0 1.0 NZ A:LYS113 4.9 28.3 1.0 HZ3 A:LYS113 4.9 0.0 1.0 H1 A:HOH683 5.0 0.0 1.0 H1 A:HOH612 5.0 0.0 1.0

U.Baumann, W.Bode, R.Huber, J.Travis, J.Potempa. Crystal Structure of Cleaved Equine Leucocyte Elastase Inhibitor Determined at 1.95 A Resolution. J.Mol.Biol. V. 226 1207 1992.
ISSN: ISSN 0022-2836
PubMed: 1518052
DOI: 10.1016/0022-2836(92)91062-T