Zinc in PDB 4mxu: Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate)

All present enzymatic activity of Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate):
3.5.1.15;

The structure of Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate), PDB code: 4mxu was solved by Y.S.Wijayasinghe, A.G.Pavlovsky, R.E.Viola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.25 / 2.60
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	146.072, 146.072, 103.424, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 23.4

The binding sites of Zinc atom in the Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate) (pdb code 4mxu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate), PDB code: 4mxu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:46.6 occ:1.00 ND1 A:HIS21 2.1 32.1 1.0 OE1 A:GLU24 2.2 46.3 1.0 OAD A:AS9402 2.4 42.8 1.0 OAG A:AS9402 2.5 43.1 1.0 OE2 A:GLU24 2.6 44.6 1.0 ND1 A:HIS116 2.7 49.1 1.0 CD A:GLU24 2.7 46.3 1.0 CE1 A:HIS21 2.8 33.0 1.0 PAM A:AS9402 2.9 45.5 1.0 CG A:HIS21 3.2 33.8 1.0 CG A:HIS116 3.3 47.8 1.0 O A:HOH509 3.4 46.3 1.0 CE1 A:HIS116 3.5 48.1 1.0 CB A:HIS116 3.5 45.0 1.0 CB A:HIS21 3.8 35.6 1.0 NH1 A:ARG63 3.9 37.3 1.0 NE2 A:HIS21 4.0 33.3 1.0 N A:AS9402 4.0 47.6 1.0 CA A:HIS116 4.1 44.4 1.0 O A:ASN117 4.2 36.7 1.0 CG A:GLU24 4.2 44.6 1.0 CA A:AS9402 4.2 48.4 1.0 CD2 A:HIS21 4.2 32.9 1.0 CD2 A:HIS116 4.3 49.6 1.0 NE2 A:HIS116 4.3 48.6 1.0 N A:ASN117 4.4 46.4 1.0 CAA A:AS9402 4.5 45.6 1.0 C A:AS9402 4.5 48.8 1.0 OXT A:AS9402 4.6 47.3 1.0 CZ A:ARG63 4.8 36.6 1.0 NH2 A:ARG63 4.8 35.9 1.0 C A:HIS116 4.8 44.0 1.0 OE2 A:GLU178 4.8 59.0 1.0 CB A:GLU24 4.8 44.9 1.0 N A:HIS21 5.0 41.0 1.0

Zinc binding site 2 out of 2 in the Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Brain Aspartoacylase Mutant K213E Complex with Intermediate Analog (N-Phosphonomethyl-L-Aspartate) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:55.7 occ:1.00 OE1 B:GLU24 2.0 45.4 1.0 OAD B:AS9402 2.0 52.4 1.0 ND1 B:HIS21 2.0 36.6 1.0 ND1 B:HIS116 2.5 54.7 1.0 CD B:GLU24 2.6 45.8 1.0 OE2 B:GLU24 2.7 49.6 1.0 CE1 B:HIS21 2.9 37.7 1.0 PAM B:AS9402 3.1 51.3 1.0 CG B:HIS21 3.1 36.8 1.0 OAG B:AS9402 3.1 50.7 1.0 CE1 B:HIS116 3.2 55.5 1.0 CG B:HIS116 3.2 50.9 1.0 CB B:HIS21 3.5 36.5 1.0 CB B:HIS116 3.6 46.3 1.0 O B:HOH507 4.0 35.8 1.0 NE2 B:HIS21 4.1 38.4 1.0 CG B:GLU24 4.1 44.9 1.0 N B:AS9402 4.1 56.8 1.0 NE2 B:HIS116 4.1 57.3 1.0 CD2 B:HIS21 4.2 37.7 1.0 CD2 B:HIS116 4.2 55.6 1.0 CA B:HIS116 4.2 44.8 1.0 NH1 B:ARG63 4.3 35.0 1.0 O B:ASN117 4.4 35.0 1.0 CA B:AS9402 4.4 59.1 1.0 CAA B:AS9402 4.5 53.2 1.0 N B:HIS21 4.5 38.6 1.0 N B:ASN117 4.6 39.1 1.0 CB B:GLU24 4.6 44.3 1.0 CA B:HIS21 4.6 38.5 1.0 C B:AS9402 4.9 58.7 1.0 NH2 B:ARG63 5.0 36.5 1.0

Y.S.Wijayasinghe, A.G.Pavlovsky, R.E.Viola. Aspartoacylase Catalytic Deficiency As the Cause of Canavan Disease: A Structural Perspective. Biochemistry V. 53 4970 2014.
ISSN: ISSN 0006-2960
PubMed: 25003821
DOI: 10.1021/BI500719K