Chlorine in PDB 4p3c: MT1-Mmp:Fab Complex (Form I)

All present enzymatic activity of MT1-Mmp:Fab Complex (Form I):
3.4.24.80;

The structure of MT1-Mmp:Fab Complex (Form I), PDB code: 4p3c was solved by H.Rozenberg, Y.Udi, I.Sagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.28 / 1.94
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.314, 80.975, 95.568, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 20

The structure of MT1-Mmp:Fab Complex (Form I) also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the MT1-Mmp:Fab Complex (Form I) (pdb code 4p3c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the MT1-Mmp:Fab Complex (Form I), PDB code: 4p3c:

Chlorine binding site 1 out of 1 in the MT1-Mmp:Fab Complex (Form I)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of MT1-Mmp:Fab Complex (Form I) within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl301 b:17.3 occ:1.00 OG H:SER52 3.0 9.6 1.0 N H:ARG56 3.4 12.2 0.4 N H:ARG56 3.4 11.9 0.6 O H:HOH492 3.5 19.6 1.0 CA H:GLY54 3.6 10.7 1.0 CB H:ARG56 3.6 13.8 0.4 C H:GLY54 3.6 14.4 1.0 CB H:ARG56 3.7 14.0 0.6 N H:GLY55 3.7 12.4 1.0 N H:GLY54 3.8 8.0 1.0 CB H:SER52 3.9 9.0 1.0 CA H:ARG56 3.9 12.7 0.4 CA H:ARG56 3.9 12.6 0.6 CG H:ARG56 4.0 15.7 0.6 N H:ASN57 4.1 11.7 1.0 ND2 H:ASN57 4.2 21.1 1.0 O H:GLY54 4.2 12.9 1.0 CG H:ARG56 4.2 15.8 0.4 C H:ARG56 4.4 12.9 0.6 C H:GLY55 4.4 13.4 1.0 C H:ARG56 4.4 12.7 0.4 CG H:ASN57 4.5 18.9 1.0 CA H:GLY55 4.6 9.2 1.0 CD H:ARG56 4.6 16.1 0.4 O H:HOH418 4.9 20.3 1.0 CB H:ASN57 4.9 15.7 1.0 O M:HOH307 4.9 21.9 1.0 CD H:ARG56 5.0 16.9 0.6

Y.Udi, M.Grossman, I.Solomonov, O.Dym, H.Rozenberg, V.Moreno, P.Cuniasse, V.Dive, A.G.Arroyo, I.Sagi. Inhibition Mechanism of Membrane Metalloprotease By An Exosite-Swiveling Conformational Antibody. Structure 2014.
ISSN: ISSN 0969-2126
PubMed: 25482542
DOI: 10.1016/J.STR.2014.10.012