Chlorine in PDB 1cws: Human CDC25B Catalytic Domain with Tungstate

The structure of Human CDC25B Catalytic Domain with Tungstate, PDB code: 1cws was solved by K.D.Watenpaugh, R.A.Reynolds, C.G.Chidester, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.734, 71.863, 74.935, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / n/a

The structure of Human CDC25B Catalytic Domain with Tungstate also contains other interesting chemical elements:

Tungsten

(W)

1 atom

The binding sites of Chlorine atom in the Human CDC25B Catalytic Domain with Tungstate (pdb code 1cws). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human CDC25B Catalytic Domain with Tungstate, PDB code: 1cws:

Chlorine binding site 1 out of 1 in the Human CDC25B Catalytic Domain with Tungstate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human CDC25B Catalytic Domain with Tungstate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl569 b:35.6 occ:1.00 O A:HOH595 2.9 26.1 1.0 O A:HOH625 3.2 44.2 1.0 N A:GLU446 3.4 16.4 1.0 N A:ARG548 3.4 32.1 1.0 CD2 A:LEU445 3.7 13.9 1.0 CG A:GLU446 3.8 29.9 1.0 CA A:LEU445 3.9 15.7 1.0 CA A:THR547 3.9 28.9 1.0 CB A:ARG548 3.9 45.9 1.0 CB A:THR547 3.9 27.3 1.0 CB A:LEU445 4.0 15.5 1.0 CB A:GLU446 4.0 22.2 1.0 C A:LEU445 4.1 16.6 1.0 C A:THR547 4.2 31.6 1.0 NH1 A:ARG447 4.3 24.1 1.0 CA A:ARG548 4.3 36.2 1.0 CA A:GLU446 4.4 20.3 1.0 CG2 A:THR547 4.4 20.8 1.0 CD A:GLU446 4.5 36.0 1.0 CG A:LEU445 4.5 16.0 1.0 N A:ARG447 4.8 20.9 1.0 O A:PRO444 4.9 19.7 1.0 OE1 A:GLU446 4.9 36.9 1.0 O A:HOH647 5.0 53.4 1.0

R.A.Reynolds, A.W.Yem, C.L.Wolfe, M.R.Deibel Jr., C.G.Chidester, K.D.Watenpaugh. Crystal Structure of the Catalytic Subunit of CDC25B Required For G2/M Phase Transition of the Cell Cycle. J.Mol.Biol. V. 293 559 1999.
ISSN: ISSN 0022-2836
PubMed: 10543950
DOI: 10.1006/JMBI.1999.3168