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Structure of the catalytic domain of USP7 (hausp)

Analyse Structure of the catalytic domain of USP7 (hausp) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NB8
Type: protein
Length: 665 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin carboxyl-terminal hydrolase 7
EC: 3.1.2.15
UniProt: Q93009
Pockets: 5 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.1.2.15)	protein	332	31% helix, 25% strand	Q93009
B	Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.1.2.15)	protein	333	32% helix, 26% strand	Q93009

Pockets

5 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	800	0.78	0.81	85	empty
2	151	0.49	0.78	20	empty
3	135	0.47	0.77	20	empty
4	135	0.40	0.74	28	empty
5	70	0.34	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 663 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

1NB8 · Structure of the catalytic domain of USP7 (HAUSP) · 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 Q93009
Elsewhere: RCSB PDB 1NB8 · PDBe 1NB8 · UniProt Q93009

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