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Bromine in PDB 5nr8: Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A

Enzymatic activity of Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A

All present enzymatic activity of Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A:
3.2.1.14;

Protein crystallography data

The structure of Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A, PDB code: 5nr8 was solved by A.Podjarny, F.Fadel, A.Golebiowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.35
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 85.897, 106.006, 42.158, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A (pdb code 5nr8). 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 Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A, PDB code: 5nr8:

Bromine binding site 1 out of 1 in 5nr8

Go back to Bromine Binding Sites List in 5nr8
Bromine binding site 1 out of 1 in the Crystal Structure of Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A


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 Human Chitotriosidase-1 (Hchit) Catalytic Domain in Complex with Compound 7A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br401

b:14.4
occ:0.70
 BR7 A:95N401 0.0 14.4 0.7
C2 A:95N401 1.9 11.9 1.0
C1 A:95N401 2.8 12.2 1.0
C3 A:95N401 2.8 12.1 1.0
CB A:MET300 3.5 13.7 0.6
CB A:THR295 3.5 13.2 1.0
CG2 A:THR295 3.6 13.5 1.0
OG1 A:THR295 3.6 13.2 1.0
CB A:MET300 3.8 10.0 0.4
N A:ALA302 3.9 9.2 1.0
C A:LEU301 4.0 9.1 1.0
N A:LEU301 4.0 9.7 1.0
C A:MET300 4.1 9.2 0.4
CD2 A:LEU362 4.1 11.0 1.0
C4 A:95N401 4.1 11.7 1.0
C6 A:95N401 4.1 10.8 1.0
C A:MET300 4.2 9.9 0.6
CA A:LEU301 4.2 9.1 1.0
O2 A:GOL406 4.3 31.3 1.0
O A:MET300 4.3 9.1 0.4
O A:LEU301 4.4 10.2 1.0
CA A:MET300 4.5 11.1 0.6
CG A:MET300 4.5 15.3 0.6
O A:MET300 4.6 10.1 0.6
CA A:ALA302 4.6 9.5 1.0
CA A:MET300 4.6 9.3 0.4
C3 A:GOL406 4.6 26.8 1.0
C5 A:95N401 4.7 11.1 1.0
O A:HOH527 4.8 12.3 1.0
OE2 A:GLU305 4.8 10.9 0.6
OE1 A:GLU305 4.9 12.2 0.4
CG A:MET300 4.9 13.1 0.4
CB A:TYR267 4.9 8.3 1.0
CB A:ALA302 4.9 10.6 1.0
CD1 A:LEU362 5.0 10.3 1.0
CA A:THR295 5.0 12.9 1.0

Reference:

M.Mazur, J.Olczak, S.Olejniczak, R.Koralewski, W.Czestkowski, A.Jedrzejczak, J.Golab, K.Dzwonek, B.Dymek, P.L.Sklepkiewicz, A.Zagozdzon, T.Noonan, K.Mahboubi, B.Conway, R.Sheeler, P.Beckett, W.M.Hungerford, A.Podjarny, A.Mitschler, A.Cousido-Siah, F.Fadel, A.Golebiowski. Targeting Acidic Mammalian Chitinase Is Effective in Animal Model of Asthma. J. Med. Chem. V. 61 695 2018.
ISSN: ISSN 1520-4804
PubMed: 29283260
DOI: 10.1021/ACS.JMEDCHEM.7B01051
Page generated: Thu Jul 11 00:31:00 2024

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