Chlorine in PDB 9cq2: Ctfab E46D Active Site Mutant Hydrolase

All present enzymatic activity of Ctfab E46D Active Site Mutant Hydrolase:
2.8.3.8; 2.8.3.9;

The structure of Ctfab E46D Active Site Mutant Hydrolase, PDB code: 9cq2 was solved by G.Buhrman, R.Bing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.19 / 2.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	131.368, 131.368, 158.423, 90, 90, 90
R / Rfree (%)	16.9 / 22

The structure of Ctfab E46D Active Site Mutant Hydrolase also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Ctfab E46D Active Site Mutant Hydrolase (pdb code 9cq2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Ctfab E46D Active Site Mutant Hydrolase, PDB code: 9cq2:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Ctfab E46D Active Site Mutant Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ctfab E46D Active Site Mutant Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:98.2 occ:1.00 H B:LYS57 2.6 35.5 1.0 HA B:PRO56 3.1 32.8 1.0 O B:HOH506 3.2 38.9 1.0 HG21 B:THR74 3.3 28.6 1.0 N B:LYS57 3.5 29.6 1.0 HB3 B:LYS57 3.7 49.2 1.0 HB2 B:TYR60 3.7 32.4 1.0 HB3 B:TYR60 3.8 32.4 1.0 CA B:PRO56 3.8 27.3 1.0 HG22 B:THR74 3.9 28.6 1.0 HB3 B:PRO56 3.9 34.3 1.0 HB2 B:LYS57 3.9 49.2 1.0 CG2 B:THR74 4.0 23.9 1.0 CB B:TYR60 4.1 27.0 1.0 O B:HOH546 4.2 36.1 1.0 CB B:LYS57 4.2 41.0 1.0 HB2 B:PRO56 4.2 34.3 1.0 C B:PRO56 4.2 23.8 1.0 CB B:PRO56 4.2 28.6 1.0 CG B:TYR60 4.3 25.1 1.0 CA B:LYS57 4.4 35.1 1.0 HG23 B:THR74 4.5 28.6 1.0 HD2 B:TYR60 4.6 32.4 1.0 CD2 B:TYR60 4.6 27.0 1.0 O B:HOH452 4.6 37.7 1.0 CD1 B:TYR60 4.9 29.5 1.0

Chlorine binding site 2 out of 3 in the Ctfab E46D Active Site Mutant Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ctfab E46D Active Site Mutant Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:67.8 occ:1.00 H C:ASP195 2.5 59.4 1.0 HB3 C:LEU194 2.9 47.0 1.0 HB C:THR193 3.1 50.5 1.0 O C:HOH491 3.1 42.1 1.0 N C:ASP195 3.3 49.5 1.0 HB2 C:ASP195 3.3 66.7 1.0 H C:LEU194 3.3 49.7 1.0 CG C:ASP195 3.6 54.6 1.0 OD1 C:ASP195 3.7 46.5 1.0 N C:LEU194 3.7 41.4 1.0 CB C:ASP195 3.8 55.5 1.0 CB C:LEU194 3.8 39.2 1.0 CB C:THR193 3.9 42.1 1.0 OD2 C:ASP195 4.0 56.4 1.0 CA C:LEU194 4.0 35.7 1.0 OG1 C:THR193 4.1 57.3 1.0 C C:LEU194 4.1 40.3 1.0 CA C:ASP195 4.1 48.5 1.0 HG1 C:THR193 4.2 68.7 1.0 HB2 C:LEU194 4.3 47.0 1.0 C C:THR193 4.4 41.1 1.0 HA C:ASP195 4.5 58.1 1.0 HG C:LEU194 4.6 67.2 1.0 CA C:THR193 4.6 50.9 1.0 HA C:THR193 4.7 61.1 1.0 HB3 C:ASP195 4.7 66.7 1.0 CG C:LEU194 4.8 56.0 1.0 HD23 C:LEU194 4.8 60.2 1.0 H C:GLU196 4.9 50.9 1.0 HG21 C:THR193 4.9 58.0 1.0 CG2 C:THR193 5.0 48.3 1.0

Chlorine binding site 3 out of 3 in the Ctfab E46D Active Site Mutant Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Ctfab E46D Active Site Mutant Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl303 b:61.7 occ:1.00 H C:LYS57 3.1 40.7 1.0 HA C:PRO56 3.6 35.4 1.0 O C:HOH488 3.6 38.5 1.0 HG22 C:THR74 3.9 29.6 1.0 HG21 C:THR74 3.9 29.6 1.0 N C:LYS57 3.9 34.0 1.0 HB2 C:TYR60 4.0 27.9 1.0 O C:HOH533 4.1 38.4 1.0 HB3 C:TYR60 4.1 27.9 1.0 HB3 C:PRO56 4.3 35.9 1.0 CG2 C:THR74 4.3 24.7 1.0 CB C:TYR60 4.4 23.3 1.0 CA C:PRO56 4.4 29.5 1.0 CG C:TYR60 4.4 27.9 1.0 CB C:LYS57 4.5 29.1 1.0 HD2 C:TYR60 4.6 31.8 1.0 CD2 C:TYR60 4.6 26.5 1.0 O C:HOH455 4.7 32.1 1.0 CB C:PRO56 4.7 29.9 1.0 HB2 C:PRO56 4.7 35.9 1.0 C C:PRO56 4.7 22.7 1.0 CA C:LYS57 4.9 37.9 1.0 HG23 C:THR74 4.9 29.6 1.0 CD1 C:TYR60 5.0 24.8 1.0

R.G.Bing, G.K.Buhrman, K.C.Ford, C.T.Straub, T.Laemthong, R.B.Rose, M.Adams, R.M.Kelly. Structural and Kinetic Characterization of An Acetoacetyl-Coenzyme A: Acetate Coenzyme A Transferase From the Extreme Thermophile Thermosipho Melanesiensis. Biochem.J. 2025.
ISSN: ESSN 1470-8728
PubMed: 39869497
DOI: 10.1042/BCJ20240747