Chlorine in PDB 1jd7: Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase

All present enzymatic activity of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase:
3.2.1.1;

The structure of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase, PDB code: 1jd7 was solved by N.Aghajari, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.70 / 2.25
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	70.300, 136.400, 113.500, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.5

The structure of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Chlorine atom in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase (pdb code 1jd7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase, PDB code: 1jd7:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl900 b:14.8 occ:1.00 O A:HOH1003 3.1 6.7 1.0 NH2 A:ARG300 3.1 13.3 1.0 NH1 A:ARG300 3.2 15.2 1.0 NH1 A:ARG172 3.2 4.1 1.0 NE A:ARG172 3.3 11.4 1.0 CZ A:ARG300 3.6 16.3 1.0 CZ A:ARG172 3.7 8.9 1.0 CG2 A:THR221 3.8 7.2 1.0 ND2 A:ASN262 4.0 16.3 1.0 CE2 A:PHE259 4.3 3.9 1.0 CZ A:PHE223 4.3 5.8 1.0 CD A:ARG172 4.5 13.1 1.0 CZ A:PHE259 4.5 4.4 1.0 CG A:GLU200 4.6 11.9 1.0 CE2 A:PHE223 4.6 3.9 1.0 CB A:ASN262 4.7 11.3 1.0 O A:HOH1511 4.7 35.7 1.0 O A:HOH1004 4.7 13.4 1.0 CB A:GLU200 4.8 9.1 1.0 CB A:THR221 4.8 9.6 1.0 CG A:ASN262 4.8 12.3 1.0 NE A:ARG300 4.9 14.5 1.0 NH2 A:ARG172 5.0 7.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl901 b:49.1 occ:1.00 O A:HOH1461 3.1 36.9 1.0 NH2 A:ARG73 3.5 19.9 1.0 NE2 A:GLN18 3.8 20.9 1.0 CD A:GLN18 4.0 22.6 1.0 CG A:GLN18 4.1 21.3 1.0 NH1 A:ARG73 4.1 16.8 1.0 CZ A:ARG73 4.2 17.9 1.0 OE1 A:GLN18 4.6 25.0 1.0

N.Aghajari, G.Feller, C.Gerday, R.Haser. Structural Basis of Alpha-Amylase Activation By Chloride Protein Sci. V. 11 1435 2002.
ISSN: ISSN 0961-8368
PubMed: 12021442
DOI: 10.1110/PS.0202602