Chlorine in PDB 4eqc: Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor

All present enzymatic activity of Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor:
2.7.11.1;

The structure of Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor, PDB code: 4eqc was solved by J.Maksimoska, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.53 / 2.01
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	51.494, 103.026, 122.350, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25.3

The binding sites of Chlorine atom in the Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor (pdb code 4eqc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor, PDB code: 4eqc:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor


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 PAK1 Kinase Domain in Complex with FRAX597 Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:24.4 occ:1.00 CL1 A:XR1601 0.0 24.4 1.0 C33 A:XR1601 1.7 24.2 1.0 C28 A:XR1601 2.7 24.5 1.0 C32 A:XR1601 2.7 23.8 1.0 C23 A:XR1601 3.0 23.0 1.0 C22 A:XR1601 3.4 24.7 1.0 N A:ARG299 3.4 20.3 1.0 O27 A:XR1601 3.5 27.1 1.0 CB A:ARG299 3.7 20.9 1.0 C A:ILE298 3.8 19.8 1.0 C24 A:XR1601 3.8 23.9 1.0 O A:ALA297 3.8 19.7 1.0 C A:ALA297 3.8 20.9 1.0 N A:ILE298 3.9 20.9 1.0 CB A:ALA297 4.0 22.6 1.0 C29 A:XR1601 4.0 23.4 1.0 CG A:MET344 4.0 20.0 1.0 C31 A:XR1601 4.0 25.5 1.0 CA A:ARG299 4.1 22.3 1.0 CA A:ILE298 4.1 19.8 1.0 CG1 A:VAL284 4.2 35.7 1.0 CG2 A:VAL284 4.2 35.6 1.0 O A:VAL342 4.3 19.1 1.0 NE A:ARG299 4.3 30.2 1.0 O A:ILE298 4.3 19.8 1.0 NH2 A:ARG299 4.5 31.0 1.0 N21 A:XR1601 4.5 24.1 1.0 CA A:ALA297 4.6 21.5 1.0 C30 A:XR1601 4.6 23.4 1.0 CB A:MET344 4.6 19.8 1.0 CZ A:ARG299 4.7 34.0 1.0 C19 A:XR1601 4.8 23.8 1.0 CB A:VAL284 4.8 36.4 1.0 CG A:ARG299 4.8 23.6 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor


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 PAK1 Kinase Domain in Complex with FRAX597 Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:33.0 occ:1.00 N A:ALA348 3.1 23.2 1.0 N A:MET399 3.2 24.6 1.0 CB A:ALA348 3.6 23.4 1.0 CA A:GLY398 3.6 22.8 1.0 CA A:ALA348 3.9 22.9 1.0 C A:GLY398 3.9 23.8 1.0 CB A:MET399 4.0 27.0 1.0 CG A:MET399 4.0 26.9 1.0 C A:LEU347 4.1 22.6 1.0 CA A:LEU347 4.1 23.1 1.0 CA A:MET399 4.2 26.1 1.0 N A:GLY349 4.3 23.5 1.0 O A:TYR346 4.4 21.8 1.0 C A:ALA348 4.5 23.0 1.0 O A:HOH915 4.7 36.1 1.0 CD2 A:LEU347 4.7 27.8 1.0 O A:LEU397 4.8 21.9 1.0 N A:GLY398 4.8 22.6 1.0 CB A:LEU347 4.9 23.2 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of PAK1 Kinase Domain in Complex with FRAX597 Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:45.5 occ:1.00 OE1 A:GLN306 3.2 36.7 1.0 N A:ASN302 3.3 27.8 1.0 NE2 A:GLN305 3.4 39.7 0.5 CG A:GLN305 3.7 39.3 0.5 CA A:MET301 3.8 26.8 1.0 CA A:GLY282 3.8 44.3 1.0 O A:ASN302 4.0 29.3 1.0 C A:MET301 4.0 26.8 1.0 CD A:GLN305 4.0 40.2 0.5 CB A:ASN302 4.1 28.9 0.5 CA A:ASN302 4.2 28.6 0.5 CA A:ASN302 4.2 28.7 0.5 CB A:ASN302 4.3 29.2 0.5 CD A:GLN306 4.3 36.9 1.0 O A:GLN300 4.3 27.2 1.0 CB A:MET301 4.4 25.8 1.0 N A:GLY282 4.5 46.1 1.0 C A:ASN302 4.5 29.4 1.0 ND2 A:ASN302 4.6 32.1 0.5 CG A:GLN306 4.6 37.3 1.0 CG A:ASN302 4.7 29.6 0.5 CG A:MET301 4.8 29.2 1.0 C A:GLY282 4.8 43.4 1.0 O A:ALA280 4.8 51.4 1.0 O A:GLY279 4.9 54.6 1.0 N A:MET301 4.9 25.5 1.0 C A:SER281 4.9 47.7 1.0 CB A:GLN305 5.0 39.3 0.5 CB A:GLN305 5.0 39.3 0.5 O A:SER281 5.0 47.7 1.0

S.Licciulli, J.Maksimoska, C.Zhou, S.Troutman, S.Kota, Q.Liu, S.Duron, D.Campbell, J.Chernoff, J.Field, R.Marmorstein, J.L.Kissil. FRAX597, A Small Molecule Inhibitor of the P21-Activated Kinases, Inhibits Tumorigenesis of Neurofibromatosis Type 2 (NF2)-Associated Schwannomas. J.Biol.Chem. V. 288 29105 2013.
ISSN: ISSN 0021-9258
PubMed: 23960073
DOI: 10.1074/JBC.M113.510933