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Chlorine in PDB 5cxa: Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470:
3.4.24.65;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470, PDB code: 5cxa was solved by C.Rouanet-Mehouas, L.Devel, V.Dive, E.A.Stura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.62 / 1.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 69.230, 63.700, 36.620, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 18.1

Other elements in 5cxa:

The structure of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470 also contains other interesting chemical elements:

Calcium (Ca) 3 atoms
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470 (pdb code 5cxa). 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 the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470, PDB code: 5cxa:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5cxa

Go back to Chlorine Binding Sites List in 5cxa
Chlorine binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470


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 the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl306

b:29.5
occ:0.86
 CL A:55L306 0.0 29.5 0.9
C14 A:55L306 1.5 21.5 0.1
C16 A:55L306 1.7 25.8 0.9
C15 A:55L306 2.3 22.1 0.1
C13 A:55L306 2.7 20.7 0.1
C15 A:55L306 2.7 25.5 0.9
C17 A:55L306 2.7 23.1 0.9
O A:HOH444 3.1 37.6 1.0
CE1 A:PHE248 3.2 19.8 1.0
CD1 A:PHE248 3.4 19.1 1.0
C16 A:55L306 3.6 22.3 0.1
O A:HOH508 3.6 33.1 1.0
O A:HOH412 3.7 29.5 1.0
CG2 A:VAL243 3.7 25.5 1.0
O A:ARG249 3.8 15.6 0.5
C12 A:55L306 3.9 19.7 0.1
C14 A:55L306 4.0 24.7 0.9
C12 A:55L306 4.0 20.1 0.9
O A:ARG249 4.0 17.2 0.5
O A:LYS233 4.1 16.8 1.0
C17 A:55L306 4.2 21.4 0.1
CG1 A:VAL243 4.3 25.9 1.0
CZ A:PHE248 4.4 20.0 1.0
C13 A:55L306 4.5 23.2 0.9
CB A:VAL243 4.5 25.2 1.0
CG A:PHE248 4.7 18.2 1.0
CL A:55L306 4.9 22.9 0.1
C A:ARG249 4.9 16.2 0.5
N A:VAL235 4.9 11.9 1.0
N A:ARG249 5.0 18.4 0.5
N A:ARG249 5.0 18.7 0.5

Chlorine binding site 2 out of 2 in 5cxa

Go back to Chlorine Binding Sites List in 5cxa
Chlorine binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470


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 the Catalytic Domain of Human MMP12 in Complex with A Carboxylate Inhibitor Related to RXP470 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl306

b:22.9
occ:0.09
 CL A:55L306 0.0 22.9 0.1
C14 A:55L306 1.6 24.7 0.9
C16 A:55L306 1.7 22.3 0.1
C15 A:55L306 2.3 25.5 0.9
C15 A:55L306 2.7 22.1 0.1
C17 A:55L306 2.7 21.4 0.1
C13 A:55L306 2.8 23.2 0.9
O A:PRO232 3.1 22.9 1.0
O A:HOH501 3.4 36.2 1.0
C16 A:55L306 3.6 25.8 0.9
CD A:LYS233 3.9 34.7 1.0
C12 A:55L306 3.9 20.1 0.9
C14 A:55L306 4.0 21.5 0.1
C12 A:55L306 4.0 19.7 0.1
CA A:LYS233 4.0 21.6 1.0
C A:PRO232 4.2 20.6 1.0
CB A:ALA241 4.2 20.7 1.0
C17 A:55L306 4.3 23.1 0.9
CG1 A:VAL243 4.3 25.9 1.0
O A:HOH520 4.4 43.4 1.0
C13 A:55L306 4.5 20.7 0.1
N A:LYS233 4.6 19.9 1.0
C A:LYS233 4.6 17.6 1.0
CE A:LYS233 4.7 37.8 1.0
O A:LYS233 4.8 16.8 1.0
CL A:55L306 4.9 29.5 0.9
CB A:LYS233 4.9 27.0 1.0

Reference:

C.Rouanet-Mehouas, B.Czarny, F.Beau, E.Cassar-Lajeunesse, E.A.Stura, V.Dive, L.Devel. Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played By the Zinc-Binding Group on Potency and Selectivity. J. Med. Chem. V. 60 403 2017.
ISSN: ISSN 1520-4804
PubMed: 27996256
DOI: 10.1021/ACS.JMEDCHEM.6B01420
Page generated: Fri Jul 26 06:19:43 2024

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