Zinc in PDB 8je0: A Novel Amidohydrolase

The structure of A Novel Amidohydrolase, PDB code: 8je0 was solved by D.Ma, R.Feng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.65 / 2.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.05, 108.05, 341.353, 90, 90, 90
R / Rfree (%)	21.4 / 25

The binding sites of Zinc atom in the A Novel Amidohydrolase (pdb code 8je0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the A Novel Amidohydrolase, PDB code: 8je0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the A Novel Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Novel Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:78.2 occ:1.00 OD1 A:ASP282 2.2 52.3 1.0 NE2 A:HIS62 2.3 48.0 1.0 NE2 A:HIS199 2.3 53.2 1.0 NE2 A:HIS64 2.3 51.3 1.0 CE1 A:HIS62 2.7 55.8 1.0 CE1 A:HIS199 2.9 47.0 1.0 CE1 A:HIS64 3.0 54.3 1.0 CG A:ASP282 3.2 59.1 1.0 NZ A:LYS164 3.4 39.6 1.0 CD2 A:HIS199 3.5 65.7 1.0 OD2 A:ASP282 3.5 62.6 1.0 CD2 A:HIS64 3.6 51.8 1.0 CD2 A:HIS62 3.6 51.7 1.0 ND1 A:HIS62 4.0 44.7 1.0 ND1 A:HIS199 4.1 59.6 1.0 ND1 A:HIS64 4.2 46.7 1.0 NE2 A:HIS222 4.2 60.4 1.0 CG A:HIS62 4.4 45.5 1.0 CG A:HIS199 4.4 71.5 1.0 CB A:ASP282 4.5 53.3 1.0 CG A:HIS64 4.5 45.1 1.0 CE1 A:HIS222 4.6 64.0 1.0 CE A:LYS164 4.7 52.8 1.0 NE A:ARG166 4.8 60.9 1.0 CB A:ALA91 4.9 41.2 1.0 O A:ALA91 4.9 43.2 1.0

Zinc binding site 2 out of 4 in the A Novel Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A Novel Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:72.6 occ:0.94 OD1 B:ASP282 2.2 57.5 1.0 NE2 B:HIS62 2.3 64.7 1.0 NE2 B:HIS199 2.3 60.2 1.0 NE2 B:HIS64 2.3 61.0 1.0 CE1 B:HIS64 2.8 57.8 1.0 CE1 B:HIS199 3.0 57.3 1.0 NZ B:LYS164 3.0 48.9 1.0 CE1 B:HIS62 3.0 62.6 1.0 CG B:ASP282 3.4 65.2 1.0 CD2 B:HIS199 3.4 62.4 1.0 CD2 B:HIS62 3.4 60.1 1.0 CD2 B:HIS64 3.6 61.8 1.0 OD2 B:ASP282 3.9 75.4 1.0 ND1 B:HIS64 4.1 47.1 1.0 ND1 B:HIS199 4.1 66.7 1.0 ND1 B:HIS62 4.3 55.6 1.0 CB B:ALA91 4.3 50.2 1.0 CG B:HIS199 4.4 68.7 1.0 CE B:LYS164 4.4 52.1 1.0 CG B:HIS64 4.5 50.6 1.0 CG B:HIS62 4.5 56.5 1.0 CB B:ASP282 4.6 54.1 1.0 O B:ALA91 4.6 53.3 1.0 NE2 B:HIS222 4.7 74.7 1.0 CE1 B:HIS222 4.7 78.6 1.0 CD B:ARG166 5.0 64.1 1.0

Zinc binding site 3 out of 4 in the A Novel Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of A Novel Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn402 b:82.4 occ:0.88 NE2 C:HIS62 2.3 53.0 1.0 NE2 C:HIS64 2.3 64.3 1.0 NE2 C:HIS199 2.4 56.2 1.0 OD1 C:ASP282 2.4 54.5 1.0 CE1 C:HIS62 2.8 63.7 1.0 CE1 C:HIS64 3.0 66.9 1.0 CE1 C:HIS199 3.2 51.4 1.0 CG C:ASP282 3.2 69.6 1.0 NZ C:LYS164 3.4 44.7 1.0 CD2 C:HIS199 3.5 64.8 1.0 OD2 C:ASP282 3.5 78.6 1.0 CD2 C:HIS62 3.6 54.2 1.0 CD2 C:HIS64 3.6 65.1 1.0 ND1 C:HIS62 4.0 52.6 1.0 NE2 C:HIS222 4.2 70.3 1.0 ND1 C:HIS64 4.2 48.8 1.0 ND1 C:HIS199 4.3 56.1 1.0 CG C:HIS62 4.4 52.9 1.0 CG C:HIS199 4.5 63.6 1.0 CG C:HIS64 4.6 50.8 1.0 CB C:ASP282 4.6 55.5 1.0 CE1 C:HIS222 4.6 73.1 1.0 CE C:LYS164 4.7 56.2 1.0 NE C:ARG166 4.7 58.5 1.0 CB C:ALA91 5.0 49.0 1.0

Zinc binding site 4 out of 4 in the A Novel Amidohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of A Novel Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn401 b:82.5 occ:1.00 OD1 D:ASP282 2.3 55.9 1.0 NE2 D:HIS62 2.3 52.6 1.0 NE2 D:HIS199 2.3 60.6 1.0 NE2 D:HIS64 2.3 45.3 1.0 CE1 D:HIS62 2.6 62.6 1.0 CE1 D:HIS64 2.8 54.5 1.0 CE1 D:HIS199 2.9 55.0 1.0 CG D:ASP282 3.3 59.7 1.0 NZ D:LYS164 3.4 49.3 1.0 CD2 D:HIS199 3.5 69.8 1.0 CD2 D:HIS62 3.6 54.4 1.0 OD2 D:ASP282 3.6 62.3 1.0 CD2 D:HIS64 3.6 55.3 1.0 ND1 D:HIS62 3.8 47.5 1.0 ND1 D:HIS64 4.1 49.3 1.0 ND1 D:HIS199 4.1 57.5 1.0 NE2 D:HIS222 4.3 62.3 1.0 CG D:HIS62 4.4 47.3 1.0 CG D:HIS199 4.5 70.7 1.0 CG D:HIS64 4.5 41.7 1.0 CD D:ARG166 4.5 53.7 1.0 CB D:ASP282 4.6 49.3 1.0 CE1 D:HIS222 4.6 68.4 1.0 CE D:LYS164 4.8 64.8 1.0 NH1 D:ARG166 4.9 61.1 1.0 CD1 D:LEU125 5.0 51.2 1.0

D.Ma, R.Feng. A Novel Amidohydrolase Catalyze the Degradation of Pam By Klebsiella Sp. Pcx To Be Published.