Research workbench

USP34 catalytic domain

Analyse USP34 catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7W3R
Type: protein
Length: 666 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 34
EC: 3.4.19.12
UniProt: Q70CQ2
Ligands: ZN
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 34 (EC 3.4.19.12)	protein	340	30% helix, 32% strand	Q70CQ2
B	Ubiquitin carboxyl-terminal hydrolase 34 (EC 3.4.19.12)	protein	326	32% helix, 30% strand	Q70CQ2

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1026	0.75	0.78	87	empty
2	108	0.42	0.77	15	empty
3	81	0.36	0.76	14	empty
4	82	0.33	0.74	17	empty
5	67	0.31	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 775 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7W3R · USP34 catalytic domain · the same entry in another collection · 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 Q70CQ2
Elsewhere: RCSB PDB 7W3R · PDBe 7W3R · UniProt Q70CQ2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.