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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 7ewx:

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

Chlorine (Cl) 3 atoms

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant), PDB code: 7ewx:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 7ewx

Go back to Manganese Binding Sites List in 7ewx
Manganese binding site 1 out of 2 in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn 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:Mn201

b:31.5
occ:1.00
O A:HOH367 2.1 30.6 1.0
OD2 A:ASP79 2.1 26.5 1.0
O A:TYR93 2.2 20.2 1.0
O A:HOH314 2.3 22.1 1.0
NE2 A:HIS34 2.4 24.1 1.0
OD1 A:ASP92 2.5 29.4 1.0
CG A:ASP79 3.1 27.6 1.0
CD2 A:HIS34 3.2 26.5 1.0
C A:TYR93 3.3 26.2 1.0
CG A:ASP92 3.3 30.9 1.0
N A:TYR93 3.4 23.8 1.0
CE1 A:HIS34 3.5 29.2 1.0
OD1 A:ASP79 3.5 26.2 1.0
OD2 A:ASP92 3.8 34.8 1.0
CA A:TYR93 3.8 24.8 1.0
O A:HOH304 4.0 28.4 1.0
C A:ASP92 4.2 25.4 1.0
CB A:TYR93 4.2 21.5 1.0
CG A:HIS34 4.4 24.0 1.0
CA A:ASP92 4.4 23.8 1.0
CB A:ASP79 4.5 21.6 1.0
NZ A:LYS94 4.5 28.6 1.0
CB A:ASP92 4.5 23.1 1.0
N A:LYS94 4.5 21.6 1.0
ND1 A:HIS34 4.5 26.1 1.0
CG A:LYS94 4.7 30.1 1.0
CD2 A:TYR93 4.8 25.8 1.0
CA A:LYS94 4.8 24.0 1.0
CG A:TYR93 4.8 25.0 1.0

Manganese binding site 2 out of 2 in 7ewx

Go back to Manganese Binding Sites List in 7ewx
Manganese binding site 2 out of 2 in the Crystal Structure of Ebinur Lake Virus Cap Snatching Endonuclease (P78A Mutant)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn 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
B:Mn201

b:49.0
occ:0.74
O B:HOH342 2.0 37.5 1.0
O B:HOH380 2.3 37.6 1.0
O B:TYR93 2.4 23.1 1.0
OD2 B:ASP79 2.5 23.4 1.0
NE2 B:HIS34 2.7 30.8 1.0
CD2 B:HIS34 3.2 25.4 1.0
CG B:ASP79 3.5 28.1 1.0
C B:TYR93 3.5 24.1 1.0
NZ B:LYS94 3.6 35.1 1.0
N B:TYR93 3.7 21.7 1.0
OD1 B:ASP79 3.7 31.7 1.0
CE1 B:HIS34 3.9 31.9 1.0
CA B:TYR93 4.1 22.1 1.0
C B:ASP92 4.3 24.9 1.0
CB B:ASP92 4.4 22.1 1.0
OD1 B:ASP92 4.4 35.1 1.0
CG B:HIS34 4.5 23.9 1.0
CD B:LYS94 4.5 33.0 1.0
CA B:ASP92 4.5 24.7 1.0
CB B:TYR93 4.5 24.4 1.0
CE B:LYS94 4.6 35.1 1.0
N B:LYS94 4.6 21.8 1.0
ND1 B:HIS34 4.8 26.7 1.0
CG B:ASP92 4.8 35.8 1.0
CB B:ASP79 4.8 26.3 1.0
CG B:LYS94 4.9 29.2 1.0
CA B:LYS94 4.9 22.5 1.0

Reference:

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
Page generated: Sun Oct 6 08:37:02 2024

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