Chlorine in PDB 7ewx: Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant)

All present enzymatic activity of Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant):
2.7.7.48;

The structure of Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant), PDB code: 7ewx was solved by W.Kuang, Z.Hu, P.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.59 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.319, 41.399, 85.776, 90, 104.94, 90
R / Rfree (%)	20.1 / 24.3

The structure of Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant) also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant) (pdb code 7ewx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant), PDB code: 7ewx:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant)


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 Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:36.7 occ:1.00 O A:HOH343 3.1 34.1 1.0 N A:VAL95 3.3 25.5 1.0 CA A:LYS94 3.6 24.0 1.0 O A:HOH367 3.7 30.6 1.0 CD2 A:HIS34 3.8 26.5 1.0 O A:HOH342 3.8 44.5 1.0 O A:VAL95 3.8 22.0 1.0 C A:LYS94 4.0 25.2 1.0 CB A:LYS94 4.0 27.3 1.0 CD A:LYS94 4.1 30.4 1.0 O A:TYR93 4.3 20.2 1.0 C A:VAL95 4.3 28.6 1.0 CG A:LYS94 4.3 30.1 1.0 CA A:VAL95 4.4 25.1 1.0 CG A:HIS34 4.5 24.0 1.0 O A:HOH347 4.5 25.6 1.0 CB A:HIS34 4.5 25.9 1.0 O A:HOH386 4.6 44.3 1.0 N A:LYS94 4.8 21.6 1.0 CB A:VAL95 4.8 26.0 1.0 NE2 A:HIS34 4.9 24.1 1.0 C A:TYR93 5.0 26.2 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant)


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 Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:49.9 occ:1.00 O A:HOH319 3.0 41.0 1.0 O A:HOH344 3.2 25.4 1.0 NZ A:LYS108 3.2 40.0 1.0 N A:THR77 3.4 25.1 1.0 CA A:VAL76 3.6 25.4 1.0 CG2 A:VAL76 3.7 30.0 1.0 CE A:LYS108 3.8 39.4 1.0 C A:VAL76 4.0 27.5 1.0 CB A:VAL76 4.1 28.1 1.0 CB A:THR77 4.3 36.0 1.0 O A:THR77 4.3 23.4 1.0 CA A:THR77 4.3 28.1 1.0 O A:HIS75 4.5 25.7 1.0 OG1 A:THR77 4.5 37.0 1.0 N A:VAL76 4.8 25.3 1.0 C A:THR77 4.8 30.0 1.0 O A:HOH394 4.8 48.7 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl202 b:31.4 occ:1.00 N B:VAL95 3.2 21.9 1.0 O B:HOH316 3.3 38.4 1.0 O B:HOH325 3.4 24.3 1.0 CD2 B:HIS34 3.8 25.4 1.0 CA B:LYS94 3.8 22.5 1.0 O B:VAL95 3.8 19.8 1.0 CB B:HIS34 3.8 22.7 1.0 C B:LYS94 4.0 23.6 1.0 CD B:LYS94 4.1 33.0 1.0 CG B:HIS34 4.1 23.9 1.0 CA B:VAL95 4.2 22.0 1.0 C B:VAL95 4.3 25.9 1.0 O B:TYR93 4.4 23.1 1.0 CB B:LYS94 4.4 25.7 1.0 CB B:VAL95 4.5 23.9 1.0 CA B:HIS34 4.7 23.5 1.0 N B:LYS94 4.8 21.8 1.0 CG B:LYS94 4.9 29.2 1.0 CG2 B:VAL95 4.9 20.9 1.0 O B:LEU30 5.0 20.4 1.0

W.Kuang, H.Zhang, Y.Cai, G.Zhang, F.Deng, H.Li, Z.Hu, Y.Guo, M.Wang, Y.Zhou, P.Gong. Insights Into Two-Metal-Ion Catalytic Mechanism of Cap-Snatching Endonuclease of Ebinur Lake Virus in Bunyavirales. J.Virol. V. 96 08521 2022.
ISSN: ESSN 1098-5514
PubMed: 35044209
DOI: 10.1128/JVI.02085-21