Chlorine in PDB 6nsq: Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L

All present enzymatic activity of Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L:
2.7.11.1;

The structure of Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L, PDB code: 6nsq was solved by P.Maisonneuve, I.Kurinov, A.Assadieskandar, C.Yu, C.Zhang, F.Sicheri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.54 / 3.05
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.543, 89.393, 112.982, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 27.5

The binding sites of Chlorine atom in the Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L (pdb code 6nsq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L, PDB code: 6nsq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl801 b:66.9 occ:1.00 CL1 B:KZP801 0.0 66.9 1.0 C18 B:KZP801 1.7 68.4 1.0 C17 B:KZP801 2.7 68.3 1.0 C20 B:KZP801 2.7 61.5 1.0 C16 B:KZP801 3.9 64.1 1.0 C21 B:KZP801 4.0 66.9 1.0 CD2 B:LEU567 4.3 51.0 1.0 CG1 B:VAL504 4.4 59.4 1.0 CD1 B:LEU567 4.5 65.2 1.0 C15 B:KZP801 4.5 62.7 1.0 CG2 B:ILE513 4.5 69.0 1.0 CD2 B:LEU505 4.7 57.7 1.0 CG2 B:THR508 4.7 41.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Braf Kinase Domain Bound to the Inhibitor 2L within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:63.5 occ:1.00 CL1 A:KZP801 0.0 63.5 1.0 C18 A:KZP801 1.7 50.5 1.0 C17 A:KZP801 2.7 47.5 1.0 C20 A:KZP801 2.7 58.9 1.0 C16 A:KZP801 3.9 58.5 1.0 C21 A:KZP801 4.0 75.3 1.0 CG1 A:VAL504 4.4 58.6 1.0 C15 A:KZP801 4.5 71.4 1.0 CD2 A:LEU567 4.6 58.3 1.0 CD2 A:LEU505 4.6 55.1 1.0 CG2 A:ILE513 4.7 41.8 1.0 CD1 A:LEU567 4.7 79.9 1.0 CG2 A:THR508 4.8 47.3 1.0

A.Assadieskandar, C.Yu, P.Maisonneuve, I.Kurinov, F.Sicheri, C.Zhang. Rigidification Dramatically Improves Inhibitor Selectivity For Raf Kinases. Acs Med.Chem.Lett. V. 10 1074 2019.
ISSN: ISSN 1948-5875
PubMed: 31312411
DOI: 10.1021/ACSMEDCHEMLETT.9B00194