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Bromine in PDB 5czm: Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470

Enzymatic activity of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470

All present enzymatic activity of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470:
3.4.24.65;

Protein crystallography data

The structure of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470, PDB code: 5czm was solved by C.Rouanet-Mehouas, L.Roselia, 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) 28.45 / 1.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.970, 63.290, 35.910, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 17.4

Other elements in 5czm:

The structure of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Calcium (Ca) 3 atoms
Chlorine (Cl) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470 (pdb code 5czm). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470, PDB code: 5czm:

Bromine binding site 1 out of 1 in 5czm

Go back to Bromine Binding Sites List in 5czm
Bromine binding site 1 out of 1 in the Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br306

b:55.4
occ:1.00
BR1 A:R47306 0.0 55.4 1.0
C22 A:R47306 1.9 34.5 1.0
C23 A:R47306 2.8 23.8 1.0
C21 A:R47306 2.9 23.4 1.0
O A:HOH664 3.1 46.3 1.0
ND1 A:HIS172 3.5 20.3 1.0
CE1 A:HIS172 4.0 22.2 1.0
O A:HOH628 4.0 40.9 1.0
O A:HOH496 4.1 10.1 0.4
C24 A:R47306 4.1 17.2 1.0
C20 A:R47306 4.2 16.4 1.0
CG A:HIS172 4.6 19.0 1.0
C19 A:R47306 4.6 13.6 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: Wed Jul 10 23:22:43 2024

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