Chlorine in PDB 8pec: Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution

All present enzymatic activity of Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution:
3.5.2.6;

The structure of Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution, PDB code: 8pec was solved by H.-K.S.Leiros, C.Frohlich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.39 / 2.66
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	202.147, 202.147, 55.699, 90, 90, 120
R / Rfree (%)	20.2 / 27.1

The binding sites of Chlorine atom in the Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution (pdb code 8pec). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution, PDB code: 8pec:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:65.5 occ:1.00 NH2 B:ARG206 3.0 45.3 1.0 NH1 A:ARG206 3.1 49.3 1.0 NH1 B:ARG206 3.3 55.8 1.0 NH2 A:ARG206 3.3 55.5 1.0 CZ B:ARG206 3.5 55.8 1.0 CZ A:ARG206 3.7 54.1 1.0 CD2 B:LEU196 3.9 57.1 1.0 CA A:GLN193 4.3 56.7 1.0 CA B:GLN193 4.3 60.6 1.0 CG A:GLN193 4.3 46.6 1.0 CB B:GLN193 4.4 57.2 1.0 CD2 A:LEU196 4.4 52.5 1.0 CB A:GLN193 4.4 52.7 1.0 CG B:GLN193 4.4 60.1 1.0 NE B:ARG206 4.9 56.8 1.0 CB A:LEU196 4.9 55.6 1.0 O B:HOH327 4.9 64.1 1.0 O A:GLN193 4.9 53.9 1.0 O B:GLN193 4.9 57.3 1.0 CG B:LEU196 5.0 57.9 1.0 NE A:ARG206 5.0 55.4 1.0

Chlorine binding site 2 out of 2 in the Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Oxa-48_Q5-Caz. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:83.7 occ:1.00 NH2 D:ARG206 2.9 79.4 1.0 NH2 C:ARG206 3.0 71.5 1.0 NH1 D:ARG206 3.4 80.2 1.0 NH1 C:ARG206 3.4 74.8 1.0 CZ D:ARG206 3.6 81.8 1.0 CZ C:ARG206 3.6 75.7 1.0 CA D:GLN193 4.1 75.0 1.0 CD2 D:LEU196 4.2 77.6 1.0 CB D:GLN193 4.2 74.0 1.0 CG D:GLN193 4.2 73.8 1.0 CA C:GLN193 4.4 79.6 1.0 CG C:GLN193 4.4 80.0 1.0 CD2 C:LEU196 4.5 82.8 1.0 CB C:GLN193 4.5 78.2 1.0 CB D:LEU196 4.8 81.8 1.0 NE D:ARG206 4.9 79.7 1.0 NE C:ARG206 4.9 78.1 1.0 CG D:LEU196 4.9 77.1 1.0 CB C:LEU196 4.9 77.9 1.0 O D:GLN193 5.0 75.1 1.0 N D:GLN193 5.0 77.4 1.0

C.Frohlich, H.-K.S.Leiros. Epistasis Arises From Shifting the Rate-Limiting Step During Enzyme Evolution. To Be Published 2024.
DOI: 10.1038/S41929-024-01117-4