Chlorine in PDB 3kff: Major Mouse Urinary Protein IV Complexed with 2-Sec-Butyl-4,5- Dihydrothiazole

The structure of Major Mouse Urinary Protein IV Complexed with 2-Sec-Butyl-4,5- Dihydrothiazole, PDB code: 3kff was solved by S.Perez-Miller, Q.Zou, T.D.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.70 / 0.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.617, 53.747, 61.249, 90.00, 90.00, 90.00
R / Rfree (%)	13.6 / 16.4

The binding sites of Chlorine atom in the Major Mouse Urinary Protein IV Complexed with 2-Sec-Butyl-4,5- Dihydrothiazole (pdb code 3kff). 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 Major Mouse Urinary Protein IV Complexed with 2-Sec-Butyl-4,5- Dihydrothiazole, PDB code: 3kff:

Chlorine binding site 1 out of 1 in the Major Mouse Urinary Protein IV Complexed with 2-Sec-Butyl-4,5- Dihydrothiazole


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Major Mouse Urinary Protein IV Complexed with 2-Sec-Butyl-4,5- Dihydrothiazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:8.0 occ:1.00 O A:HOH559 3.1 16.6 1.0 O A:HOH502 3.2 9.0 1.0 N A:ARG156 3.3 6.7 1.0 N A:LEU158 3.6 8.3 1.0 CG A:LEU158 3.6 7.8 1.0 N A:CYS157 3.8 7.6 1.0 OD1 A:ASN155 3.9 9.5 1.0 CB A:LEU158 3.9 8.2 1.0 CD1 A:LEU158 4.0 9.8 1.0 O A:THR154 4.0 7.3 1.0 CA A:ARG156 4.1 7.3 1.0 CA A:ASN155 4.2 7.8 1.0 C A:ARG156 4.2 7.5 1.0 CB A:ARG156 4.2 6.9 1.0 C A:ASN155 4.2 7.2 1.0 CA A:LEU158 4.4 8.2 1.0 O A:HOH566 4.5 18.3 1.0 CA A:CYS157 4.6 8.7 1.0 C A:CYS157 4.6 8.1 1.0 CG A:ASN155 4.8 8.3 1.0 CD2 A:LEU158 4.9 9.4 1.0 C A:THR154 5.0 6.9 1.0

S.Perez-Miller, Q.Zou, M.V.Novotny, T.D.Hurley. High Resolution X-Ray Structures of Mouse Major Urinary Protein Nasal Isoform in Complex with Pheromones. Protein Sci. V. 19 1469 2010.
ISSN: ISSN 0961-8368
PubMed: 20509168
DOI: 10.1002/PRO.426