Zinc in PDB 2x3b: ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase

All present enzymatic activity of ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase:
3.4.24.39;

The structure of ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase, PDB code: 2x3b was solved by X.Bogdanovic, G.J.Palm, R.K.Singh, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	91.81 / 2.28
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.855, 60.196, 183.612, 90.00, 90.00, 90.00
R / Rfree (%)	24.4 / 29.3

The binding sites of Zinc atom in the ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase (pdb code 2x3b). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase, PDB code: 2x3b:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1341 b:35.4 occ:1.00 OD2 A:ASP306 1.9 38.2 1.0 NE2 A:HIS297 1.9 20.7 1.0 NE2 A:HIS293 2.1 26.6 1.0 O A:HOH2139 2.4 2.0 1.0 CG A:ASP306 2.7 36.6 1.0 CE1 A:HIS297 2.8 21.6 1.0 OD1 A:ASP306 2.8 33.8 1.0 CD2 A:HIS293 2.9 24.6 1.0 CD2 A:HIS297 3.0 20.2 1.0 CE1 A:HIS293 3.2 26.4 1.0 N B:LYS85 3.5 28.0 1.0 C B:ILE84 3.5 27.9 1.0 O B:ILE84 3.7 28.0 1.0 N B:ILE84 3.9 28.0 1.0 ND1 A:HIS297 3.9 23.3 1.0 CA B:LYS85 4.0 28.0 1.0 CG A:HIS297 4.0 21.6 1.0 CG A:HIS293 4.1 23.4 1.0 CB A:ASP306 4.1 38.4 1.0 C B:LEU83 4.1 28.1 1.0 CA B:ILE84 4.2 27.7 1.0 CB B:LYS85 4.2 27.4 1.0 ND1 A:HIS293 4.2 24.7 1.0 CB A:ALA329 4.3 22.8 1.0 O B:LEU83 4.3 28.2 1.0 CB B:LEU83 4.4 27.4 1.0 CA B:LEU83 4.9 28.0 1.0 O A:HIS293 5.0 20.9 1.0 CE1 A:TYR309 5.0 37.4 1.0

Zinc binding site 2 out of 2 in the ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of ASAP1 Inactive Mutant E294A, An Extracellular Toxic Zinc Metalloendopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1341 b:31.9 occ:1.00 OD2 B:ASP306 1.9 29.9 1.0 NE2 B:HIS297 1.9 20.5 1.0 NE2 B:HIS293 2.0 21.9 1.0 O B:HOH2116 2.4 5.2 1.0 CG B:ASP306 2.7 30.8 1.0 OD1 B:ASP306 2.8 30.9 1.0 CD2 B:HIS297 2.8 20.5 1.0 CD2 B:HIS293 2.9 20.0 1.0 CE1 B:HIS297 3.0 20.6 1.0 CE1 B:HIS293 3.1 19.8 1.0 O A:ILE84 3.4 27.0 1.0 C A:ILE84 3.5 27.0 1.0 N A:LYS85 3.6 27.2 1.0 N A:ILE84 3.9 26.1 1.0 CG B:HIS297 4.0 22.4 1.0 CA A:LYS85 4.0 27.6 1.0 ND1 B:HIS297 4.0 21.1 1.0 CG B:HIS293 4.1 20.8 1.0 CB B:ASP306 4.1 30.6 1.0 C A:LEU83 4.1 25.8 1.0 ND1 B:HIS293 4.1 20.3 1.0 CA A:ILE84 4.2 26.7 1.0 CB B:ALA329 4.2 24.5 1.0 CB A:LYS85 4.3 27.4 1.0 O A:LEU83 4.4 26.7 1.0 CB A:LEU83 4.4 24.2 1.0 CE1 B:TYR309 4.7 32.8 1.0 CA A:LEU83 4.9 24.9 1.0 OH B:TYR309 4.9 31.9 1.0

X.Bogdanovic, G.J.Palm, J.Schwenteit, R.K.Singh, B.K.Gudmundsdottir, W.Hinrichs. Structural Evidence of Intramolecular Propeptide Inhibition of the Aspzincin Metalloendopeptidase ASAP1. Febs Lett. V. 590 3280 2016.
ISSN: ISSN 0014-5793
PubMed: 27528449
DOI: 10.1002/1873-3468.12356