Arsenic in PDB 6e66: Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb

The structure of Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb, PDB code: 6e66 was solved by Q.Yao, Y.Q.Zheng, F.Shao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.74 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.587, 101.458, 38.636, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.1

The binding sites of Arsenic atom in the Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb (pdb code 6e66). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 3 binding sites of Arsenic where determined in the Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb, PDB code: 6e66:
Jump to Arsenic binding site number: 1; 2; 3;

Arsenic binding site 1 out of 3 in the Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb within 5.0Å range: probe atom residue distance (Å) B Occ A:As190 b:43.6 occ:1.00 AS A:CAS190 0.0 43.6 1.0 CE2 A:CAS190 2.0 34.5 1.0 CE1 A:CAS190 2.0 30.5 1.0 SG A:CAS190 2.3 32.1 1.0 CB A:CAS190 3.2 27.8 1.0 OG A:SER188 3.6 37.8 1.0 N A:CAS190 3.6 32.5 1.0 CA A:CAS190 4.0 33.5 1.0 CD A:PRO189 4.2 33.0 1.0 CB A:PRO189 4.4 32.6 1.0 C A:PRO189 4.5 33.7 1.0 CG A:PRO189 4.5 36.6 1.0 N A:PRO189 4.6 34.4 1.0 CA A:PRO189 4.8 30.5 1.0 CB A:SER188 4.8 37.0 1.0

Arsenic binding site 2 out of 3 in the Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb within 5.0Å range: probe atom residue distance (Å) B Occ A:As221 b:69.9 occ:1.00 AS A:CAS221 0.0 69.9 1.0 CE1 A:CAS221 1.9 57.0 1.0 CE2 A:CAS221 2.0 48.0 1.0 SG A:CAS221 2.3 60.3 1.0 CB A:CAS221 3.4 54.1 1.0 N A:CAS221 4.1 60.8 1.0 O A:VAL219 4.1 55.2 1.0 OH A:TYR279 4.2 56.8 1.0 C A:ASP220 4.2 58.3 1.0 CA A:CAS221 4.3 59.1 1.0 CE2 A:PHE282 4.4 34.1 1.0 CA A:ASP220 4.6 54.8 1.0 O A:ASP220 4.6 62.8 1.0 CA A:GLY264 4.6 32.8 1.0 CG1 A:VAL219 4.6 51.7 1.0 CE1 A:TYR279 4.6 46.9 1.0 C A:VAL219 4.6 58.0 1.0 CG2 A:VAL217 4.7 35.7 1.0 N A:ASP220 4.8 60.8 1.0 CZ A:TYR279 4.9 47.6 1.0 CD2 A:PHE282 4.9 36.1 1.0 O A:GLY264 5.0 25.0 1.0

Arsenic binding site 3 out of 3 in the Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Crystal Structure of Bacterial N-Acetylglucosamine Transferase Nleb within 5.0Å range: probe atom residue distance (Å) B Occ A:As283 b:70.9 occ:1.00 AS A:CAS283 0.0 70.9 1.0 CE2 A:CAS283 2.0 50.7 1.0 CE1 A:CAS283 2.0 58.6 1.0 SG A:CAS283 2.3 60.7 1.0 CB A:CAS283 3.3 34.2 1.0 O A:VAL219 3.5 55.2 1.0 CE2 A:CAS221 3.6 48.0 1.0 CA A:CAS283 3.7 30.1 1.0 OH A:TYR279 4.1 56.8 1.0 OE1 A:GLU287 4.2 60.5 1.0 O A:CAS283 4.4 32.8 1.0 C A:CAS283 4.5 38.5 1.0 OD1 A:ASP220 4.6 62.8 1.0 CZ A:TYR279 4.6 47.6 1.0 C A:VAL219 4.7 58.0 1.0 CD A:GLU287 4.7 63.2 1.0 OE2 A:GLU287 4.8 71.8 1.0 CE2 A:TYR279 4.8 42.6 1.0 N A:VAL219 4.9 52.2 1.0 N A:CAS283 5.0 29.2 1.0

J.Ding, X.Pan, L.Du, Q.Yao, J.Xue, H.Yao, D.C.Wang, S.Li, F.Shao. Structural and Functional Insights Into Host Death Domains Inactivation By the Bacterial Arginine Glcnacyltransferase Effector. Mol.Cell V. 74 922 2019.
ISSN: ISSN 1097-2765
PubMed: 30979585
DOI: 10.1016/J.MOLCEL.2019.03.028