Chlorine in PDB 4cc3: Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3

The structure of Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3, PDB code: 4cc3 was solved by L.Polle, L.Rigano, R.Julian, K.Ireton, W.-D.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.33 / 1.97
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	115.870, 115.870, 73.080, 90.00, 90.00, 120.00
R / Rfree (%)	18.084 / 21.508

The binding sites of Chlorine atom in the Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3 (pdb code 4cc3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3, PDB code: 4cc3:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl2576 b:51.0 occ:1.00 O A:HOH2002 3.1 46.4 1.0 N A:SER1533 3.3 32.8 1.0 O A:HOH2016 3.3 51.6 1.0 CA A:LEU1532 3.8 33.2 1.0 O A:GLU1531 3.8 30.9 1.0 C A:LEU1532 4.0 33.2 1.0 OG A:SER1533 4.0 33.0 1.0 O A:HOH2012 4.1 53.5 1.0 CB A:SER1533 4.1 34.8 1.0 CB A:ALA1526 4.1 29.6 1.0 CD1 A:LEU1532 4.2 41.9 1.0 CA A:SER1533 4.3 34.2 1.0 O A:HOH2018 4.5 39.7 1.0 C A:GLU1531 4.6 30.1 1.0 N A:LEU1532 4.6 31.6 1.0 CB A:LEU1532 4.8 34.1 1.0 CG A:LEU1532 4.8 35.8 1.0 O A:SER1533 5.0 37.8 1.0

Chlorine binding site 2 out of 3 in the Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl2576 b:51.0 occ:1.00 O C:HOH2032 3.1 46.0 1.0 NH1 C:ARG1527 3.1 36.8 1.0 N C:LYS1525 3.1 33.6 1.0 OH A:TYR1518 3.8 53.4 1.0 CB C:LYS1525 3.8 36.5 1.0 NH2 C:ARG1527 3.9 40.9 1.0 O C:HOH2009 3.9 44.1 1.0 O A:HOH2037 3.9 35.4 1.0 CZ C:ARG1527 3.9 38.5 1.0 CA C:PHE1524 3.9 37.2 1.0 C C:PHE1524 4.0 35.7 1.0 CA C:LYS1525 4.0 35.5 1.0 CE2 A:TYR1518 4.0 46.5 1.0 O C:LYS1525 4.1 37.8 1.0 CD1 C:PHE1524 4.2 32.6 1.0 CG C:LYS1525 4.2 40.1 1.0 O C:THR1523 4.4 43.1 1.0 CZ A:TYR1518 4.4 49.9 1.0 C C:LYS1525 4.5 33.0 1.0 CH2 A:TRP1555 4.8 34.7 1.0 CE1 C:PHE1524 4.8 32.8 1.0 N C:PHE1524 4.8 35.6 1.0 CG C:PHE1524 4.9 34.5 1.0 CB C:PHE1524 4.9 37.5 1.0 C C:THR1523 4.9 41.5 1.0

Chlorine binding site 3 out of 3 in the Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Complex of Human Tuba C-Terminal SH3 Domain and Mena Proline-Rich Peptide - H3 within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl2576 b:48.3 occ:1.00 O E:HOH2002 3.2 45.4 1.0 N E:SER1533 3.2 37.7 1.0 NZ E:LYS1562 3.3 59.4 1.0 O C:HOH2026 3.3 35.8 1.0 OG E:SER1533 3.8 36.9 1.0 CB E:SER1533 3.8 40.4 1.0 CA E:LEU1532 3.9 35.4 1.0 O E:GLU1531 4.0 35.0 1.0 O E:HOH2015 4.0 48.8 1.0 C E:LEU1532 4.0 34.8 1.0 CA E:SER1533 4.1 36.8 1.0 CD1 E:LEU1532 4.1 40.5 1.0 CB E:ALA1526 4.2 36.2 1.0 CE E:LYS1562 4.2 70.0 1.0 O E:HOH2014 4.4 44.6 1.0 CD E:LYS1562 4.4 65.6 1.0 O E:HOH2017 4.5 42.6 1.0 N E:LEU1532 4.7 35.0 1.0 C E:GLU1531 4.7 32.3 1.0 CG E:LEU1532 4.8 38.0 1.0 O E:SER1533 4.8 37.8 1.0 CB E:LEU1532 4.8 34.4 1.0 CG2 C:THR1552 4.8 37.4 1.0

L.Polle, L.A.Rigano, R.Julian, K.Ireton, W.Schubert. Structural Details of Human Tuba Recruitment By Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading. Structure V. 22 304 2014.
ISSN: ISSN 0969-2126
PubMed: 24332715
DOI: 10.1016/J.STR.2013.10.017