Chlorine in PDB 1sce: Crystal Structure of the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch

The structure of Crystal Structure of the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch, PDB code: 1sce was solved by Y.Bourne, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.700, 85.600, 97.700, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 28.4

The binding sites of Chlorine atom in the Crystal Structure of the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch (pdb code 1sce). 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 the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch, PDB code: 1sce:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch


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 the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl981 b:22.2 occ:1.00 OG A:SER79 2.8 24.9 1.0 O A:HOH868 2.8 40.3 1.0 NH2 C:ARG99 2.9 28.2 1.0 OG1 B:THR77 2.9 15.2 1.0 NH2 B:ARG72 3.5 5.0 1.0 CB A:SER79 3.7 18.2 1.0 NH1 C:ARG99 3.7 28.6 1.0 CZ C:ARG99 3.7 28.9 1.0 CB B:THR77 3.8 13.3 1.0 O B:HOH797 3.9 25.0 1.0 CZ B:ARG72 4.4 11.3 1.0 CA B:THR77 4.5 11.6 1.0 NE B:ARG72 4.5 11.6 1.0 O A:LEU80 4.7 14.5 1.0 O A:HOH762 4.8 18.1 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch


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 the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl983 b:18.5 occ:1.00 NE1 B:TRP82 3.0 10.5 1.0 O A:HOH754 3.1 2.0 1.0 OG1 A:THR77 3.2 12.4 1.0 N B:SER79 3.3 12.4 1.0 NH1 B:ARG39 3.4 12.9 1.0 CB B:GLN78 3.5 19.3 1.0 O A:THR77 3.6 10.5 1.0 C A:THR77 3.7 8.7 1.0 CG2 A:THR77 3.8 2.5 1.0 CD1 B:TRP82 3.8 10.2 1.0 CA B:GLN78 3.8 13.0 1.0 N A:GLN78 3.9 10.5 1.0 CB A:THR77 4.0 9.7 1.0 OG B:SER79 4.0 28.1 1.0 CA A:GLN78 4.0 8.1 1.0 C B:GLN78 4.0 13.4 1.0 CE2 B:TRP82 4.1 8.8 1.0 CB B:SER79 4.1 17.4 1.0 CA B:SER79 4.3 17.6 1.0 CZ B:ARG39 4.4 8.2 1.0 C A:GLN78 4.4 6.4 1.0 CA A:THR77 4.5 9.9 1.0 CZ2 B:TRP82 4.6 8.3 1.0 NH2 B:ARG39 4.6 8.9 1.0 NE2 B:GLN78 4.6 18.2 1.0 CG B:GLN78 4.7 18.4 1.0 O B:HOH783 4.7 10.4 1.0 O A:GLN78 4.8 6.5 1.0 NH1 D:ARG99 4.9 31.3 1.0 N A:SER79 5.0 7.0 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch


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 the Cell Cycle Regulatory Protein SUC1 Reveals A Novel Beta-Hinge Conformational Switch within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl984 b:15.6 occ:1.00 O C:HOH896 2.8 15.0 1.0 N C:HIS88 3.0 15.6 1.0 ND1 C:HIS88 3.3 6.8 1.0 CA C:VAL87 3.7 12.7 1.0 C C:VAL87 3.8 16.2 1.0 CA C:HIS88 3.9 13.7 1.0 CB C:HIS88 3.9 6.3 1.0 O C:HIS88 3.9 16.5 1.0 CG C:HIS88 4.0 9.0 1.0 CB C:VAL87 4.3 11.7 1.0 O C:GLU86 4.3 19.1 1.0 CE1 C:HIS88 4.4 9.5 1.0 C C:HIS88 4.4 14.5 1.0 CG1 C:VAL87 4.7 16.6 1.0 N C:VAL87 4.8 11.9 1.0 CG1 A:VAL87 4.9 25.2 1.0 O C:VAL87 5.0 15.7 1.0

Y.Bourne, A.S.Arvai, S.L.Bernstein, M.H.Watson, S.I.Reed, J.E.Endicott, M.E.Noble, L.N.Johnson, J.A.Tainer. Crystal Structure of the Cell Cycle-Regulatory Protein SUC1 Reveals A Beta-Hinge Conformational Switch. Proc.Natl.Acad.Sci.Usa V. 92 10232 1995.
ISSN: ISSN 0027-8424
PubMed: 7479758
DOI: 10.1073/PNAS.92.22.10232