Chlorine in PDB 5e98: Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A

All present enzymatic activity of Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A:
3.2.1.166;

The structure of Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A, PDB code: 5e98 was solved by L.Wu, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.42 / 1.63
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.790, 71.290, 77.920, 90.00, 95.06, 90.00
R / Rfree (%)	17.3 / 20

The binding sites of Chlorine atom in the Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A (pdb code 5e98). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A, PDB code: 5e98:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl604 b:66.8 occ:1.00 NH1 A:ARG334 3.7 43.1 1.0 NZ A:LYS337 3.7 38.6 1.0 CD A:ARG334 3.7 35.3 1.0 CE A:LYS337 4.1 39.4 1.0 CA A:GLU288 4.2 40.9 1.0 O A:GLY287 4.3 35.8 1.0 CZ A:ARG334 4.6 40.8 1.0 NE A:ARG334 4.6 37.8 1.0 N A:GLU288 4.7 35.3 1.0 C A:GLY287 4.7 35.2 1.0 CG A:ARG334 4.8 36.0 1.0 CG A:GLU288 4.8 61.9 1.0 CB A:ARG334 4.8 33.4 1.0 O A:HOH740 4.8 53.2 1.0 CB A:GLU288 4.8 49.9 1.0 O A:GLU288 4.9 43.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Heparanase in Complex with Hepmer M04S02A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl605 b:65.3 occ:1.00 N A:THR416 3.4 26.6 1.0 O A:HOH857 3.5 37.0 1.0 CA A:GLY415 3.6 24.5 1.0 OD1 A:ASN439 3.6 33.7 1.0 OG1 A:THR416 3.7 28.2 1.0 N A:THR440 3.7 39.2 1.0 OG1 A:THR440 3.8 55.0 1.0 O A:HOH851 3.8 37.0 1.0 CA A:ASN439 3.8 27.5 1.0 CG2 A:THR416 3.9 26.2 1.0 C A:GLY415 4.0 27.4 1.0 CB A:THR416 4.2 26.0 1.0 CG A:ASN439 4.3 31.1 1.0 C A:ASN439 4.3 29.4 1.0 CA A:THR416 4.4 26.0 1.0 CG2 A:THR440 4.5 54.7 1.0 CB A:ASN439 4.6 26.9 1.0 CB A:THR440 4.6 49.2 1.0 O A:THR438 4.6 30.2 1.0 CA A:THR440 4.7 47.0 1.0 N A:ASN439 4.8 27.7 1.0 N A:GLY415 4.9 23.5 1.0

L.Wu, C.M.Viola, A.M.Brzozowski, G.J.Davies. Structural Characterization of Human Heparanase Reveals Insights Into Substrate Recognition. Nat.Struct.Mol.Biol. V. 22 1016 2015.
ISSN: ESSN 1545-9985
PubMed: 26575439
DOI: 10.1038/NSMB.3136