Chlorine in PDB 8jug: Crystal Structure of Human Mmp-7 in Complex with Inhibitor

All present enzymatic activity of Crystal Structure of Human Mmp-7 in Complex with Inhibitor:
3.4.24.23;

The structure of Crystal Structure of Human Mmp-7 in Complex with Inhibitor, PDB code: 8jug was solved by M.Kamitani, K.Abe-Sato, Y.Oka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.05 / 1.30
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	76.06, 76.06, 61.89, 90, 90, 90
R / Rfree (%)	22.1 / 23.8

The structure of Crystal Structure of Human Mmp-7 in Complex with Inhibitor also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Fluorine	(F)	6 atoms
Zinc	(Zn)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor (pdb code 8jug). 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 Mmp-7 in Complex with Inhibitor, PDB code: 8jug:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor


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 Mmp-7 in Complex with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1 b:18.8 occ:0.50 CL1 C:7SF1 0.0 18.8 0.5 CL1 C:7SF1 0.0 14.7 0.5 C40 C:7SF1 1.8 15.3 0.5 C40 C:7SF1 1.8 12.7 0.5 C42 C:7SF1 2.7 12.9 0.5 C42 C:7SF1 2.7 15.5 0.5 C39 C:7SF1 2.7 14.9 0.5 C39 C:7SF1 2.8 12.7 0.5 F45 C:7SF1 2.9 13.9 0.5 F45 C:7SF1 2.9 17.5 0.5 C44 C:7SF1 3.0 13.6 0.5 F46 C:7SF1 3.1 13.7 0.5 C44 C:7SF1 3.1 16.7 0.5 F46 C:7SF1 3.1 17.3 0.5 CG A:HIS214 3.5 9.2 1.0 ND1 A:HIS214 3.6 9.8 1.0 CB A:HIS214 3.7 9.1 1.0 CE2 A:TYR210 3.8 16.0 1.0 O A:HOH428 3.9 16.0 1.0 CD2 A:HIS214 3.9 9.1 1.0 C43 C:7SF1 4.0 12.0 0.5 C43 C:7SF1 4.0 13.8 0.5 C38 C:7SF1 4.0 14.4 0.5 C38 C:7SF1 4.1 12.7 0.5 CE1 A:HIS214 4.1 9.8 1.0 CD1 A:TYR236 4.1 16.4 1.0 CA A:TYR236 4.2 19.7 1.0 CB A:TYR236 4.2 18.6 1.0 CD2 A:TYR210 4.2 13.8 1.0 N A:TYR236 4.3 18.4 1.0 NE2 A:HIS214 4.3 9.4 1.0 F47 C:7SF1 4.3 13.6 0.5 F47 C:7SF1 4.4 16.8 0.5 O A:THR235 4.5 19.9 1.0 C A:THR235 4.5 20.2 1.0 C37 C:7SF1 4.6 11.7 0.5 C37 C:7SF1 4.6 12.8 0.5 CG A:TYR236 4.6 17.1 1.0 O A:VAL231 4.9 10.7 1.0 CA A:ALA211 5.0 9.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor


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 Mmp-7 in Complex with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1 b:14.7 occ:0.50 CL1 C:7SF1 0.0 14.7 0.5 CL1 C:7SF1 0.0 18.8 0.5 C40 C:7SF1 1.8 15.3 0.5 C40 C:7SF1 1.8 12.7 0.5 C39 C:7SF1 2.7 14.9 0.5 C39 C:7SF1 2.7 12.7 0.5 C42 C:7SF1 2.7 12.9 0.5 C42 C:7SF1 2.7 15.5 0.5 F45 C:7SF1 2.9 13.9 0.5 F45 C:7SF1 3.0 17.5 0.5 C44 C:7SF1 3.1 13.6 0.5 F46 C:7SF1 3.1 13.7 0.5 C44 C:7SF1 3.1 16.7 0.5 F46 C:7SF1 3.1 17.3 0.5 CG A:HIS214 3.5 9.2 1.0 ND1 A:HIS214 3.6 9.8 1.0 CB A:HIS214 3.7 9.1 1.0 CE2 A:TYR210 3.8 16.0 1.0 O A:HOH428 3.9 16.0 1.0 CD2 A:HIS214 3.9 9.1 1.0 C43 C:7SF1 4.0 12.0 0.5 C43 C:7SF1 4.0 13.8 0.5 C38 C:7SF1 4.0 14.4 0.5 C38 C:7SF1 4.0 12.7 0.5 CE1 A:HIS214 4.0 9.8 1.0 CD1 A:TYR236 4.1 16.4 1.0 CA A:TYR236 4.2 19.7 1.0 CB A:TYR236 4.2 18.6 1.0 CD2 A:TYR210 4.2 13.8 1.0 N A:TYR236 4.3 18.4 1.0 NE2 A:HIS214 4.3 9.4 1.0 F47 C:7SF1 4.4 13.6 0.5 F47 C:7SF1 4.4 16.8 0.5 O A:THR235 4.5 19.9 1.0 C A:THR235 4.5 20.2 1.0 C37 C:7SF1 4.6 11.7 0.5 C37 C:7SF1 4.6 12.8 0.5 CG A:TYR236 4.6 17.1 1.0 O A:VAL231 4.9 10.7 1.0 CA A:ALA211 5.0 9.4 1.0

K.Abe-Sato, H.Tabuse, H.Kanazawa, M.Kamitani, M.Endo, S.Tokura, S.Wakabayashi, T.Yahara, T.Takeda, K.Hitaka, E.Gunji, N.Kojima, Y.Oka. Structure-Based Optimization and Biological Evaluation of Potent and Selective Mmp-7 Inhibitors For Kidney Fibrosis. J.Med.Chem. 2023.
ISSN: ISSN 0022-2623
PubMed: 37861435
DOI: 10.1021/ACS.JMEDCHEM.3C01166