Chlorine in PDB 8cqg: Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis

All present enzymatic activity of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis:
3.2.1.1;

The structure of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis, PDB code: 8cqg was solved by S.Skagseth, B.A.Lund, J.J.Griese, F.Van Der Ent, J.Aqvist, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.48 / 1.74
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.879, 80.93, 128.481, 90, 90, 90
R / Rfree (%)	17.7 / 20.5

The structure of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis (pdb code 8cqg). 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 of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis, PDB code: 8cqg:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis


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 A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl512 b:27.1 occ:1.00 HE A:ARG172 2.4 29.8 1.0 HH12 A:ARG300 2.5 29.8 1.0 HH22 A:ARG300 2.5 31.7 1.0 HH21 A:ARG172 2.5 31.4 1.0 HD22 A:ASN262 2.6 33.5 1.0 HG21 A:THR221 3.0 29.0 1.0 HG3 A:GLU200 3.2 33.6 1.0 NH1 A:ARG300 3.2 24.9 1.0 NE A:ARG172 3.2 24.9 1.0 O A:HOH870 3.2 25.4 1.0 NH2 A:ARG300 3.3 26.4 1.0 NH2 A:ARG172 3.3 26.2 1.0 ND2 A:ASN262 3.5 28.0 1.0 HZ A:PHE223 3.5 25.8 1.0 CZ A:ARG300 3.7 25.8 1.0 CZ A:ARG172 3.7 28.5 1.0 HD21 A:ASN262 3.8 33.5 1.0 HG22 A:THR221 3.8 29.0 1.0 CG2 A:THR221 3.9 24.2 1.0 HH11 A:ARG300 3.9 29.8 1.0 HH21 A:ARG300 4.0 31.7 1.0 HB2 A:GLU200 4.0 31.4 1.0 HH22 A:ARG172 4.0 31.4 1.0 HB2 A:ASN262 4.0 31.4 1.0 CG A:GLU200 4.1 28.0 1.0 CZ A:PHE223 4.2 21.5 1.0 HD2 A:ARG172 4.2 28.8 1.0 HE2 A:PHE198 4.3 36.0 1.0 CD A:ARG172 4.3 24.0 1.0 HB3 A:ASN262 4.4 31.4 1.0 HG23 A:THR221 4.4 29.0 1.0 HZ A:PHE259 4.4 32.9 1.0 HE1 A:PHE223 4.5 26.5 1.0 CG A:ASN262 4.5 23.3 1.0 HE1 A:PHE259 4.5 32.4 1.0 CB A:ASN262 4.5 26.2 1.0 CB A:GLU200 4.6 26.2 1.0 CZ A:PHE259 4.6 27.4 1.0 CE1 A:PHE259 4.6 27.0 1.0 HB A:THR221 4.6 32.5 1.0 HE22 A:GLN33 4.6 29.1 1.0 HG2 A:GLU200 4.7 33.6 1.0 CE1 A:PHE223 4.7 22.1 1.0 HA A:GLU200 4.7 31.0 1.0 O A:HOH677 4.9 27.2 1.0 CB A:THR221 4.9 27.1 1.0 HG3 A:ARG172 4.9 31.7 1.0 CD A:GLU200 4.9 29.1 1.0 OE2 A:GLU200 5.0 28.4 1.0 HE1 A:HIS263 5.0 42.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl513 b:35.0 occ:1.00 H A:LEU57 2.4 32.6 1.0 HH11 A:ARG64 2.5 35.9 1.0 HD2 A:ARG64 2.6 38.8 1.0 O A:HOH977 2.9 38.4 1.0 HA A:GLU56 2.9 30.6 1.0 N A:LEU57 3.2 27.2 1.0 NH1 A:ARG64 3.2 29.9 1.0 HG A:LEU57 3.5 34.5 1.0 HB2 A:LEU57 3.5 32.9 1.0 HB3 A:GLU56 3.6 39.2 1.0 CD A:ARG64 3.6 32.4 1.0 HH12 A:ARG64 3.6 35.9 1.0 HB2 A:ARG64 3.6 32.6 1.0 CA A:GLU56 3.7 25.5 1.0 C A:GLU56 4.0 27.1 1.0 CB A:LEU57 4.1 27.4 1.0 HD3 A:ARG64 4.1 38.8 1.0 CB A:GLU56 4.1 32.7 1.0 CZ A:ARG64 4.2 32.8 1.0 CG A:LEU57 4.2 28.8 1.0 HG2 A:GLU56 4.2 44.2 1.0 CA A:LEU57 4.2 23.9 1.0 HG3 A:ARG64 4.2 34.8 1.0 NE A:ARG64 4.3 31.0 1.0 CG A:ARG64 4.3 29.0 1.0 CB A:ARG64 4.4 27.2 1.0 HD12 A:LEU57 4.5 34.6 1.0 CG A:GLU56 4.7 36.9 1.0 HB3 A:ARG64 4.8 32.6 1.0 O A:TYR55 4.8 31.4 1.0 O A:HOH631 4.9 42.5 1.0 C A:LEU57 4.9 29.2 1.0 CD1 A:LEU57 4.9 28.9 1.0 N A:GLU56 4.9 27.0 1.0 HB2 A:GLU56 4.9 39.2 1.0 HA A:LEU57 4.9 28.7 1.0 O A:HOH720 5.0 33.3 1.0 HB3 A:LEU57 5.0 32.9 1.0

F.Van Der Ent, S.Skagseth, B.Lund, J.Socan, J.Griese, B.O.Brandsdal, J.Aqvist. Computational Design of the Temperature Optimum of An Enzyme Reaction Sci Adv 2023.
ISSN: ESSN 2375-2548
DOI: 10.1126/SCIADV.ADI0963