Chlorine in PDB 5lmf: Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500)

The structure of Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500), PDB code: 5lmf was solved by C.Charenton, C.Gaudon-Plesse, Z.Fourati, V.Taverniti, R.Back, O.Kolesnikova, B.Seraphin, M.Graille, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.48 / 2.15
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	98.360, 122.920, 126.970, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24.6

The structure of Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500) also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500) (pdb code 5lmf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500), PDB code: 5lmf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1002 b:67.5 occ:1.00 CB A:ASN620 3.6 49.5 1.0 CA A:ASN620 3.7 47.4 1.0 CG A:ASN620 4.1 64.0 1.0 N A:ASN620 4.2 48.3 1.0 ND2 A:ASN620 4.3 59.6 1.0 C A:ASN619 4.7 52.3 1.0 O A:ASN619 4.7 53.4 1.0 OD1 A:ASN620 4.8 53.2 1.0

Chlorine binding site 2 out of 2 in the Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of C-Terminal Domain From S. Cerevisiae PAT1 Decapping Activator Bound to DCP2 HLM3 Peptide (Region 484-500) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl801 b:61.3 occ:1.00 O1 B:EDO807 3.3 58.8 1.0 N B:LEU578 3.4 46.6 1.0 O B:HOH928 3.7 40.2 1.0 CB B:THR577 3.8 51.1 1.0 CA B:THR577 3.9 46.3 1.0 C1 B:EDO807 3.9 57.7 1.0 C B:THR577 4.1 49.7 1.0 CB B:LEU578 4.1 45.8 1.0 CG2 A:THR760 4.2 43.0 1.0 CA B:LEU578 4.4 45.6 1.0 CD2 B:LEU693 4.4 54.0 1.0 CD1 B:LEU693 4.4 50.7 1.0 CG2 B:THR577 4.5 50.1 1.0 C2 B:EDO807 4.6 57.5 1.0 OG1 B:THR577 5.0 47.7 1.0

C.Charenton, C.Gaudon-Plesse, Z.Fourati, V.Taverniti, R.Back, O.Kolesnikova, B.Seraphin, M.Graille. A Unique Surface on PAT1 C-Terminal Domain Directly Interacts with DCP2 Decapping Enzyme and XRN1 5'-3' Mrna Exonuclease in Yeast. Proc. Natl. Acad. Sci. V. 114 E9493 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29078363
DOI: 10.1073/PNAS.1711680114