Zinc in PDB 7w6x: Crystal Structure of E. Coli Rsep in Complex with Batimastat

The structure of Crystal Structure of E. Coli Rsep in Complex with Batimastat, PDB code: 7w6x was solved by K.Takanuki, Y.Imaizumi, T.Nogi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.76 / 3.20
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	47.34, 56.12, 69.67, 68.17, 74.59, 69.35
R / Rfree (%)	24.6 / 30.5

The binding sites of Zinc atom in the Crystal Structure of E. Coli Rsep in Complex with Batimastat (pdb code 7w6x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of E. Coli Rsep in Complex with Batimastat, PDB code: 7w6x:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of E. Coli Rsep in Complex with Batimastat


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of E. Coli Rsep in Complex with Batimastat within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:74.8 occ:1.00 OD2 A:ASP402 2.0 90.3 1.0 NE2 A:HIS26 2.1 81.5 1.0 OD1 A:ASP402 2.1 82.6 1.0 NE2 A:HIS22 2.1 70.5 1.0 O2 A:BAT502 2.2 72.8 1.0 O1 A:BAT502 2.2 80.3 1.0 CG A:ASP402 2.3 84.4 1.0 CE1 A:HIS22 2.7 70.5 1.0 N1 A:BAT502 2.9 65.3 1.0 C2 A:BAT502 2.9 77.7 1.0 CE1 A:HIS26 3.0 76.2 1.0 CD2 A:HIS26 3.1 76.0 1.0 CD2 A:HIS22 3.4 73.3 1.0 CB A:ASP402 3.8 79.6 1.0 ND1 A:HIS22 3.9 71.8 1.0 ND1 A:HIS26 4.1 74.0 1.0 CG A:HIS26 4.2 75.3 1.0 CG A:HIS22 4.3 71.8 1.0 C1 A:BAT502 4.4 76.4 1.0 CA A:GLY104 4.6 55.2 1.0 CD A:PRO105 4.6 69.4 1.0 O A:ILE101 4.6 80.3 1.0 CA A:ASP402 4.8 76.8 1.0 N A:ASP402 4.9 75.4 1.0 C8 A:BAT502 5.0 68.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of E. Coli Rsep in Complex with Batimastat


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of E. Coli Rsep in Complex with Batimastat within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:92.1 occ:1.00 NE2 A:HIS86 2.0 87.4 1.0 NE2 A:HIS87 2.0 82.0 1.0 CD2 A:HIS87 2.8 82.6 1.0 CE1 A:HIS86 2.9 85.7 1.0 CD2 A:HIS86 3.1 88.6 1.0 CE1 A:HIS87 3.2 85.2 1.0 ND1 A:HIS86 4.0 83.8 1.0 CG A:HIS87 4.0 76.6 1.0 ND1 A:HIS87 4.2 78.3 1.0 CG A:HIS86 4.2 84.8 1.0 O A:GLU83 4.3 86.4 1.0 OE2 A:GLU83 4.3 98.7 1.0 CD A:GLU83 4.8 104.6 1.0 CG A:GLU83 5.0 104.8 1.0

Y.Imaizumi, K.Takanuki, T.Miyake, M.Takemoto, K.Hirata, M.Hirose, R.Oi, T.Kobayashi, K.Miyoshi, R.Aruga, T.Yokoyama, S.Katagiri, H.Matsuura, K.Iwasaki, T.Kato, M.K.Kaneko, Y.Kato, M.Tajiri, S.Akashi, O.Nureki, Y.Hizukuri, Y.Akiyama, T.Nogi. Mechanistic Insights Into Intramembrane Proteolysis By E. Coli Site-2 Protease Homolog Rsep. Sci Adv V. 8 P9011 2022.
ISSN: ESSN 2375-2548
PubMed: 36001659
DOI: 10.1126/SCIADV.ABP9011