MolNFT v1 · #72686 · protein

Crystal structure of murine aminoacylase 3 in complex with N-acetyl-L- tyrosine

3NFZ · Aspartoacylase-2: “Crystal structure of murine aminoacylase 3 in complex with N-acetyl-L- tyrosine”. X-ray diffraction, 3 ligands (3NF, ZN, CL), 1 pocket (best druggability 0.77). MolNFT v1 #72686 on GenesisL1: 3D structure, binding…

PDB: 3NFZ
Type: protein
Length: 305 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartoacylase-2
EC: 3.5.1.-
UniProt: Q91XE4
Ligands: 3NF, ZN, CL
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartoacylase-2 (EC 3.5.1.-)	protein	305	28% helix, 26% strand	Q91XE4

Ligands and binding sites

3NF · N-acetyl-L-tyrosine · ligand · chains A
ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.77	0.97	23	3NF

Compared structures

3NFZ · Crystal structure of murine aminoacylase 3 in complex with N-acetyl-L-tyrosine · the same entry in another collection · chain A against A, TM-score 1.00
Q91XE4 · AlphaFold monomer V2.0 prediction for N-acyl-aromatic-L-amino acid amidohydrolase… · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q91XE4
Elsewhere: RCSB PDB 3NFZ · PDBe 3NFZ · UniProt Q91XE4

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