Chlorine in PDB 4p3d: MT1-Mmp:Fab Complex (Form II)

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

The structure of MT1-Mmp:Fab Complex (Form II), PDB code: 4p3d 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)	39.66 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.898, 96.226, 81.521, 90.00, 92.36, 90.00
R / Rfree (%)	15.8 / 21

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

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the MT1-Mmp:Fab Complex (Form II) (pdb code 4p3d). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the MT1-Mmp:Fab Complex (Form II), PDB code: 4p3d:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the MT1-Mmp:Fab Complex (Form II)


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 II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:14.9 occ:1.00 OG A:SER52 3.0 9.2 1.0 N A:ARG56 3.4 9.4 0.4 N A:ARG56 3.4 9.2 0.6 CB A:ARG56 3.4 11.1 0.4 O A:HOH437 3.5 15.7 1.0 CA A:GLY54 3.6 8.8 1.0 CB A:ARG56 3.6 11.6 0.6 C A:GLY54 3.7 9.8 1.0 N A:GLY55 3.8 11.8 1.0 CA A:ARG56 3.9 10.2 0.4 CA A:ARG56 3.9 10.1 0.6 N A:GLY54 3.9 9.6 1.0 N A:ASN57 4.0 8.2 1.0 CB A:SER52 4.0 8.1 1.0 CG A:ARG56 4.0 11.6 0.4 CG A:ARG56 4.1 9.7 0.6 C A:ARG56 4.3 10.1 0.6 ND2 A:ASN57 4.3 18.7 1.0 O A:GLY54 4.3 10.9 1.0 C A:ARG56 4.4 10.1 0.4 CD A:ARG56 4.4 11.8 0.4 C A:GLY55 4.5 10.3 1.0 CG A:ASN57 4.6 16.6 1.0 CA A:GLY55 4.7 7.8 1.0 CB A:ASN57 4.9 12.3 1.0 CD A:ARG56 4.9 11.0 0.6 O A:HOH413 5.0 18.2 1.0

Chlorine binding site 2 out of 2 in the MT1-Mmp:Fab Complex (Form II)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of MT1-Mmp:Fab Complex (Form II) within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl301 b:16.3 occ:1.00 OG H:SER52 3.0 9.1 1.0 O H:HOH488 3.3 22.8 1.0 N H:ARG56 3.4 11.8 0.4 N H:ARG56 3.4 11.6 0.6 CB H:ARG56 3.5 14.3 0.4 CA H:GLY54 3.6 9.2 1.0 C H:GLY54 3.7 11.8 1.0 N H:GLY55 3.7 11.7 1.0 N H:GLY54 3.8 8.8 1.0 CB H:ARG56 3.9 14.4 0.6 CB H:SER52 3.9 9.1 1.0 CA H:ARG56 3.9 12.7 0.4 CA H:ARG56 4.0 12.5 0.6 CG H:ARG56 4.0 14.4 0.4 N H:ASN57 4.0 8.8 1.0 CG H:ARG56 4.3 14.3 0.6 ND2 H:ASN57 4.3 13.8 1.0 O H:GLY54 4.3 12.1 1.0 C H:ARG56 4.3 11.7 0.6 CD H:ARG56 4.4 13.8 0.4 C H:ARG56 4.4 11.5 0.4 C H:GLY55 4.4 12.1 1.0 CG H:ASN57 4.5 11.6 1.0 CA H:GLY55 4.6 8.4 1.0 CB H:ASN57 4.8 9.5 1.0 CD H:ARG56 4.9 13.6 0.6 O H:HOH417 4.9 16.0 1.0 O M:HOH405 4.9 16.2 1.0 O M:HOH408 5.0 18.4 1.0

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