Chlorine in PDB 1t0h: Crystal Structure of the Rattus Norvegicus Voltage Gated Calcium Channel Beta Subunit Isoform 2A

The structure of Crystal Structure of the Rattus Norvegicus Voltage Gated Calcium Channel Beta Subunit Isoform 2A, PDB code: 1t0h was solved by F.Van Petegem, K.Clark, F.Chatelain, D.Minor Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.05 / 1.97
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	36.176, 45.260, 58.701, 107.34, 95.75, 97.00
R / Rfree (%)	18.5 / 21.3

The binding sites of Chlorine atom in the Crystal Structure of the Rattus Norvegicus Voltage Gated Calcium Channel Beta Subunit Isoform 2A (pdb code 1t0h). 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 Crystal Structure of the Rattus Norvegicus Voltage Gated Calcium Channel Beta Subunit Isoform 2A, PDB code: 1t0h:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Rattus Norvegicus Voltage Gated Calcium Channel Beta Subunit Isoform 2A


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 Rattus Norvegicus Voltage Gated Calcium Channel Beta Subunit Isoform 2A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:38.5 occ:1.00 CD A:ARG134 3.6 43.2 1.0 CA A:HIS131 3.7 31.4 1.0 CB A:HIS131 3.9 32.1 1.0 ND1 A:HIS131 3.9 36.4 1.0 N A:HIS131 4.0 30.4 1.0 CG A:GLN130 4.1 34.0 1.0 NE A:ARG134 4.1 46.9 1.0 CG A:HIS131 4.4 33.8 1.0 C A:GLN130 4.4 29.8 1.0 O A:GLN130 4.5 29.7 1.0 O A:HOH234 4.6 39.0 1.0 OE1 A:GLN130 4.7 42.7 1.0 CD A:GLN130 4.7 37.6 1.0 CG A:ARG134 4.8 40.0 1.0 CB A:ARG134 4.9 38.0 1.0 CB A:GLN130 4.9 30.0 1.0 C A:HIS131 5.0 31.3 1.0

F.Van Petegem, K.A.Clark, F.C.Chatelain, D.L.Minor. Structure of A Complex Between A Voltage-Gated Calcium Channel Beta-Subunit and An Alpha-Subunit Domain. Nature V. 429 671 2004.
ISSN: ISSN 0028-0836
PubMed: 15141227
DOI: 10.1038/NATURE02588