Zinc in PDB 8c0j: Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain

All present enzymatic activity of Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain:
3.5.1.28;

The structure of Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain, PDB code: 8c0j was solved by A.Crow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 3.38
Space group	I 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	237.363, 237.363, 237.363, 90, 90, 90
R / Rfree (%)	24.9 / 29.1

The binding sites of Zinc atom in the Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain (pdb code 8c0j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain, PDB code: 8c0j:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:94.8 occ:1.00 NE2 A:HIS200 1.9 91.5 1.0 OE1 A:GLU215 2.0 68.4 1.0 ND1 A:HIS269 2.1 101.4 1.0 CE1 A:HIS200 2.9 104.3 1.0 CD A:GLU215 2.9 75.7 1.0 CD2 A:HIS200 2.9 94.3 1.0 CE1 A:HIS269 3.0 115.9 1.0 CG A:HIS269 3.1 86.9 1.0 OE2 A:GLU215 3.2 95.0 1.0 CB A:HIS269 3.5 79.0 1.0 O A:ALA270 3.9 128.1 1.0 ND1 A:HIS200 4.0 104.2 1.0 CG A:HIS200 4.0 97.1 1.0 NE2 A:HIS269 4.2 102.5 1.0 CD2 A:HIS269 4.2 85.8 1.0 CG A:GLU215 4.3 80.3 1.0 CA A:HIS269 4.5 76.1 1.0 N A:ALA270 4.6 83.9 1.0 OE2 A:GLU382 4.8 92.4 1.0 C A:ALA270 4.9 98.8 1.0 OE1 A:GLU382 4.9 99.1 1.0

Zinc binding site 2 out of 2 in the Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Amib Enzymatic Domain Bound to the Envc Lytm Domain within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn501 b:138.7 occ:1.00 NE2 C:HIS200 1.8 121.6 1.0 OE1 C:GLU215 2.0 128.4 1.0 ND1 C:HIS269 2.1 103.0 1.0 CE1 C:HIS200 2.8 134.0 1.0 CD2 C:HIS200 2.8 126.8 1.0 CD C:GLU215 2.9 128.2 1.0 CE1 C:HIS269 3.0 105.0 1.0 CG C:HIS269 3.1 113.5 1.0 OE2 C:GLU215 3.1 151.6 1.0 CB C:HIS269 3.6 123.0 1.0 ND1 C:HIS200 3.9 131.7 1.0 CG C:HIS200 4.0 119.5 1.0 O C:ALA270 4.0 122.4 1.0 NE2 C:HIS269 4.1 100.8 1.0 CD2 C:HIS269 4.2 102.4 1.0 CG C:GLU215 4.3 119.3 1.0 CA C:HIS269 4.5 106.3 1.0 N C:ALA270 4.6 117.0 1.0 OE2 C:GLU382 5.0 128.7 1.0

J.Cook, T.C.Baverstock, M.B.L.Mcandrew, D.I.Roper, P.J.Stansfeld, A.Crow. Activator-Induced Conformational Changes Regulate Division-Associated Peptidoglycan Amidases. Proc.Natl.Acad.Sci.Usa V. 120 80120 2023.
ISSN: ESSN 1091-6490
PubMed: 37276423
DOI: 10.1073/PNAS.2302580120