Chlorine in PDB 3ha1: Alanine Racemase From Bacillus Anthracis (Ames)

All present enzymatic activity of Alanine Racemase From Bacillus Anthracis (Ames):
5.1.1.1;

The structure of Alanine Racemase From Bacillus Anthracis (Ames), PDB code: 3ha1 was solved by R.M.Counago, M.Davlieva, U.Strych, R.E.Hill, K.L.Krause, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.79 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.624, 141.271, 60.124, 90.00, 103.11, 90.00
R / Rfree (%)	16 / 20.1

The binding sites of Chlorine atom in the Alanine Racemase From Bacillus Anthracis (Ames) (pdb code 3ha1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Alanine Racemase From Bacillus Anthracis (Ames), PDB code: 3ha1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Alanine Racemase From Bacillus Anthracis (Ames)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Alanine Racemase From Bacillus Anthracis (Ames) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl399 b:26.1 occ:1.00 NH2 A:ARG138 3.2 22.9 1.0 NE A:ARG138 3.2 19.7 1.0 O A:HOH422 3.3 11.2 1.0 O A:HOH400 3.3 13.9 1.0 ND2 A:ASN131 3.3 25.7 1.0 O A:HOH402 3.4 14.3 1.0 CZ A:ARG138 3.6 25.2 1.0 CB A:HIS168 4.1 20.7 1.0 CG1 A:ILE139 4.1 26.0 1.0 O A:ILE139 4.1 22.9 1.0 CB A:ARG138 4.1 22.5 1.0 CG A:MET136 4.3 22.5 1.0 N A:ILE139 4.3 22.1 1.0 CG A:ASN131 4.3 24.9 1.0 OD1 A:ASN131 4.4 25.5 1.0 CD A:ARG138 4.4 21.8 1.0 CG A:ARG138 4.4 24.9 1.0 CG A:HIS168 4.6 23.9 1.0 CD2 A:HIS168 4.6 20.8 1.0 CB A:MET136 4.7 19.3 1.0 C2' A:LLP41 4.7 25.7 1.0 C A:ILE139 4.8 22.4 1.0 NH1 A:ARG138 5.0 19.8 1.0 CA A:ILE139 5.0 22.8 1.0

Chlorine binding site 2 out of 2 in the Alanine Racemase From Bacillus Anthracis (Ames)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Alanine Racemase From Bacillus Anthracis (Ames) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl399 b:29.5 occ:1.00 NE B:ARG138 3.2 27.0 1.0 O B:HOH473 3.2 12.0 1.0 NH2 B:ARG138 3.3 27.7 1.0 O B:HOH400 3.3 14.1 1.0 ND2 B:ASN131 3.4 25.2 1.0 O B:HOH490 3.4 17.4 1.0 CZ B:ARG138 3.7 29.8 1.0 CG1 B:ILE139 4.0 28.0 1.0 CB B:HIS168 4.1 25.8 1.0 O B:ILE139 4.2 28.4 1.0 CG B:MET136 4.2 23.2 1.0 CB B:ARG138 4.3 26.7 1.0 N B:ILE139 4.3 25.5 1.0 CD B:ARG138 4.3 25.9 1.0 CG B:ASN131 4.4 27.7 1.0 CG B:ARG138 4.4 24.9 1.0 OD1 B:ASN131 4.4 30.4 1.0 CG B:HIS168 4.6 26.1 1.0 CB B:MET136 4.6 23.6 1.0 CD2 B:HIS168 4.7 27.0 1.0 CD1 B:ILE139 4.8 29.2 1.0 C B:ILE139 4.8 27.9 1.0 C2' B:LLP41 5.0 29.0 1.0

R.M.Counago, M.Davlieva, U.Strych, R.E.Hill, K.L.Krause. Biochemical and Structural Characterization of Alanine Racemase From Bacillus Anthracis (Ames). Bmc Struct.Biol. V. 9 53 2009.
ISSN: ESSN 1472-6807
PubMed: 19695097
DOI: 10.1186/1472-6807-9-53