Bromine in PDB 6e4l: The Structure of the N-Terminal Domain of Human Clathrin Heavy Chain 1 (Ntd) in Complex with ES9

The structure of The Structure of the N-Terminal Domain of Human Clathrin Heavy Chain 1 (Ntd) in Complex with ES9, PDB code: 6e4l was solved by W.Dejonghe, I.Sharma, B.Denoo, S.D.Munck, H.Bulut, E.Mylle, M.Vasileva, Q.Lu, D.V.Savatin, K.Mishev, W.Nerinckx, A.Staes, A.Drozdzecki, D.Audenaert, A.Madder, J.Friml, D.V.Damme, K.Gevaert, V.Haucke, S.Savvides, J.Winne, E.Russinova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.42 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.210, 74.340, 84.230, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 21.4

The binding sites of Bromine atom in the The Structure of the N-Terminal Domain of Human Clathrin Heavy Chain 1 (Ntd) in Complex with ES9 (pdb code 6e4l). 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 The Structure of the N-Terminal Domain of Human Clathrin Heavy Chain 1 (Ntd) in Complex with ES9, PDB code: 6e4l:

Bromine binding site 1 out of 1 in the The Structure of the N-Terminal Domain of Human Clathrin Heavy Chain 1 (Ntd) in Complex with ES9


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of The Structure of the N-Terminal Domain of Human Clathrin Heavy Chain 1 (Ntd) in Complex with ES9 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br409 b:69.2 occ:0.86 BR A:HRS409 0.0 69.2 0.9 CAE A:HRS409 1.9 43.1 0.9 CAD A:HRS409 2.9 40.2 0.9 HG3 A:GLN89 3.1 38.0 1.0 HAD A:HRS409 3.1 48.3 0.9 SAA A:HRS409 3.2 54.2 0.9 HB2 A:LEU82 3.2 34.4 1.0 HB2 A:GLN89 3.3 32.7 1.0 HB3 A:LEU82 3.5 34.4 1.0 O A:LEU82 3.7 24.5 1.0 CG A:GLN89 3.8 31.7 1.0 CB A:LEU82 3.8 28.7 1.0 HB3 A:ALA84 3.8 37.7 1.0 C A:LEU82 3.8 22.8 1.0 HB2 A:ALA84 3.9 37.7 1.0 HA A:LYS83 3.9 29.9 1.0 CB A:GLN89 4.0 27.2 1.0 HE2 A:PHE91 4.0 32.8 0.6 H A:ALA84 4.1 35.6 1.0 CAC A:HRS409 4.1 48.5 0.9 H A:GLN89 4.1 26.5 1.0 N A:LYS83 4.1 24.3 1.0 HE21 A:GLN89 4.2 52.7 1.0 N A:ALA84 4.2 29.7 1.0 C A:LYS83 4.3 27.4 1.0 CB A:ALA84 4.3 31.4 1.0 CD A:GLN89 4.3 46.5 1.0 HG22 A:THR87 4.3 39.4 1.0 CA A:LYS83 4.3 24.9 1.0 CAB A:HRS409 4.3 49.6 0.9 O A:THR87 4.4 31.5 1.0 NE2 A:GLN89 4.4 43.9 1.0 N A:GLN89 4.4 22.1 1.0 CA A:LEU82 4.5 25.5 1.0 H A:LYS83 4.6 29.2 1.0 HG2 A:GLN89 4.6 38.0 1.0 HD12 A:LEU82 4.6 38.8 1.0 HD13 A:LEU82 4.7 38.8 1.0 HA A:LEU88 4.7 28.7 1.0 HB3 A:GLN89 4.7 32.7 1.0 HB2 A:ALA68 4.8 44.1 1.0 O A:LYS83 4.8 31.2 1.0 CA A:GLN89 4.8 20.0 1.0 CA A:ALA84 4.9 33.7 1.0 CE2 A:PHE91 4.9 27.3 0.6 HE22 A:GLN89 5.0 52.7 1.0 CD1 A:LEU82 5.0 32.3 1.0 HZ A:PHE91 5.0 33.1 0.6

W.Dejonghe, I.Sharma, B.Denoo, S.De Munck, Q.Lu, K.Mishev, H.Bulut, E.Mylle, R.De Rycke, M.Vasileva, D.V.Savatin, W.Nerinckx, A.Staes, A.Drozdzecki, D.Audenaert, K.Yperman, A.Madder, J.Friml, D.Van Damme, K.Gevaert, V.Haucke, S.N.Savvides, J.Winne, E.Russinova. Disruption of Endocytosis Through Chemical Inhibition of Clathrin Heavy Chain Function. Nat.Chem.Biol. V. 15 641 2019.
ISSN: ESSN 1552-4469
PubMed: 31011214
DOI: 10.1038/S41589-019-0262-1