Chlorine in PDB 4wmv: Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A

The structure of Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A, PDB code: 4wmv was solved by M.C.Clifton, A.Moulin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	98.890, 136.070, 37.820, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 25.3

The structure of Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A (pdb code 4wmv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A, PDB code: 4wmv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:50.6 occ:1.00 O A:MET134 3.5 32.6 1.0 OD1 A:ASN136 3.7 20.8 1.0 N A:ASN136 3.7 36.1 1.0 CG A:ASN136 3.7 19.6 1.0 CA A:PRO135 3.9 25.0 1.0 ND2 A:ASN136 4.0 22.3 1.0 C A:PRO135 4.1 22.4 1.0 CB A:ASN136 4.3 22.4 1.0 O A:ASP-101 4.4 25.5 1.0 C A:MET134 4.5 12.8 1.0 O A:ALA-100 4.5 25.0 1.0 CD2 A:HIS-132 4.6 12.4 1.0 CA A:ALA-100 4.6 14.0 1.0 N A:PRO135 4.6 22.6 1.0 CA A:ASN136 4.7 23.6 1.0 OH A:TYR-20 4.7 46.0 1.0 NE2 A:HIS-132 4.7 27.7 1.0 C A:ALA-100 4.9 18.6 1.0 CE2 A:TYR-20 5.0 43.4 1.0

Chlorine binding site 2 out of 2 in the Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Mbp-MCL1 Bound to Ligand 4 at 2.4A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:89.2 occ:1.00 CL14 A:3R4404 0.0 89.2 1.0 C13 A:3R4404 1.7 65.6 1.0 C04 A:3R4404 2.7 72.9 1.0 C12 A:3R4404 2.8 55.1 1.0 C11 A:3R4404 3.2 45.1 1.0 C02 A:3R4404 3.2 63.8 1.0 O03 A:3R4404 3.3 40.2 1.0 CA A:LEU267 3.6 27.1 1.0 CB A:LEU267 3.6 24.6 1.0 N A:LEU267 3.9 19.6 1.0 CD1 A:LEU267 3.9 17.4 1.0 CD1 A:PHE254 4.0 43.3 1.0 C06 A:3R4404 4.0 56.9 1.0 O01 A:3R4404 4.2 72.8 1.0 S05 A:3R4404 4.2 72.0 1.0 CG A:LEU267 4.4 28.8 1.0 O A:ARG263 4.4 26.5 1.0 CE1 A:PHE254 4.5 42.1 1.0 C10 A:3R4404 4.5 59.0 1.0 C A:THR266 4.6 27.2 1.0 CG2 A:THR266 4.6 19.2 1.0 SD A:MET250 4.6 0.6 1.0 CG A:PHE254 4.9 44.8 1.0 CB A:THR266 4.9 31.1 1.0 O A:THR266 4.9 17.1 1.0 C A:LEU267 5.0 21.5 1.0

M.C.Clifton, D.M.Dranow, A.Leed, B.Fulroth, J.W.Fairman, J.Abendroth, K.A.Atkins, E.Wallace, D.Fan, G.Xu, Z.J.Ni, D.Daniels, J.Van Drie, G.Wei, A.B.Burgin, T.R.Golub, B.K.Hubbard, M.H.Serrano-Wu. A Maltose-Binding Protein Fusion Construct Yields A Robust Crystallography Platform For MCL1. Plos One V. 10 25010 2015.
ISSN: ESSN 1932-6203
PubMed: 25909780
DOI: 10.1371/JOURNAL.PONE.0125010