GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the first two ubl domains of deubiquitylase USP7

Analyse Crystal structure of the first two ubl domains of deubiquitylase USP7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PYZ
Type
protein
Length
524 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin carboxyl-terminal hydrolase 7
EC
3.4.19.12
UniProt
Q93009
Ligands
UNX
Pockets
3 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)protein26333% helix, 29% strandQ93009
BUbiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12)protein26129% helix, 29% strandQ93009

Ligands and binding sites

  • UNX · Unknown atom or ion · ion · 2 copies · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111290.810.82113empty
2770.320.7418empty
3530.300.7617empty

Interfaces

1 interface between chains.

  • A–B · 865 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4PYZ · Crystal structure of the first two Ubl domains of Deubiquitylase USP7 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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