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Crystal structure of the dub domain of human amsh-lp

Analyse Crystal structure of the dub domain of human amsh-lp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZNR
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amsh-like protease
EC: 3.1.2.15
UniProt: Q96FJ0
Ligands: ZN, PR
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amsh-like protease (EC 3.1.2.15)	protein	178	28% helix, 35% strand	Q96FJ0

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
PR · Praseodymium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 7 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.40	0.80	17	empty

Compared structures

2ZNR · Crystal structure of the DUB domain of human AMSH-LP · the same entry in another collection · chain A against A, TM-score 1.00
Q96FJ0 · AlphaFold monomer V2.0 prediction for amsh-like protease (Q96FJ0) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q96FJ0
Elsewhere: RCSB PDB 2ZNR · PDBe 2ZNR · UniProt Q96FJ0

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