Chlorine in PDB 4wmu: Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A

The structure of Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A, PDB code: 4wmu was solved by M.C.Clifton, J.W.Faiman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.46 / 1.55
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	98.870, 135.900, 37.680, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 19

The structure of Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A (pdb code 4wmu). 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 2 at 1.55A, PDB code: 4wmu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A


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 2 at 1.55A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:24.9 occ:1.00 CL2 A:19H402 0.0 24.9 1.0 CAT A:19H402 1.8 26.1 1.0 CAG A:19H402 2.7 22.8 1.0 CAK A:19H402 2.8 26.4 1.0 O A:ALA227 3.5 19.5 1.0 CB A:MET231 3.6 25.1 1.0 CD1 A:PHE228 3.7 12.8 1.0 C A:ALA227 3.8 19.8 1.0 CAH A:19H402 4.0 19.6 1.0 CB A:ALA227 4.0 17.7 1.0 CAY A:19H402 4.1 28.2 1.0 CE A:MET231 4.1 43.8 1.0 N A:PHE228 4.1 15.4 1.0 CG A:MET231 4.2 29.2 1.0 CE1 A:PHE228 4.2 12.3 1.0 O A:HOH610 4.3 39.9 1.0 CA A:PHE228 4.3 15.3 1.0 CA A:ALA227 4.5 20.3 1.0 CAZ A:19H402 4.6 21.8 1.0 SD A:MET231 4.8 39.5 1.0 CG A:PHE228 4.9 12.6 1.0 CA A:MET231 4.9 21.1 1.0

Chlorine binding site 2 out of 2 in the Structure of Mbp-MCL1 Bound to Ligand 2 at 1.55A


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 2 at 1.55A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:21.5 occ:1.00 CL1 A:19H402 0.0 21.5 1.0 CAV A:19H402 1.7 18.9 1.0 CAS A:19H402 2.7 15.9 1.0 CAR A:19H402 2.7 16.7 1.0 CAB A:19H402 3.0 19.2 1.0 CAA A:19H402 3.1 22.2 1.0 CD1 A:LEU246 3.7 24.7 1.0 CD2 A:LEU246 3.9 24.2 1.0 CE2 A:PHE270 3.9 18.5 1.0 CAJ A:19H402 4.0 16.4 1.0 CAI A:19H402 4.0 17.8 1.0 CB A:LEU246 4.0 20.1 1.0 CG A:LEU246 4.1 20.7 1.0 CG A:MET250 4.1 24.8 1.0 CD2 A:PHE270 4.2 17.0 1.0 CD1 A:LEU235 4.2 27.9 1.0 SD A:MET250 4.5 27.4 1.0 CAU A:19H402 4.5 17.1 1.0 CD1 A:ILE237 4.8 29.5 1.0 CG2 A:VAL274 4.8 15.5 1.0 CE A:MET250 5.0 22.8 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