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Structure of a conserved dimerisation domain within FBOX7 and PI31

Analyse Structure of a conserved dimerisation domain within FBOX7 and PI31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VT8
Type: protein
Length: 286 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteasome inhibitor PI31 subunit
UniProt: Q92530
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proteasome inhibitor PI31 subunit	protein	143	32% helix, 29% strand	Q92530
B	Proteasome inhibitor PI31 subunit	protein	143	32% helix, 29% strand	Q92530

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.46	0.81	19	empty
2	139	0.43	0.75	31	empty

Interfaces

1 interface between chains.

A–B · 320 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (oxidation).

Compared structures

2VT8 · Structure of a conserved dimerisation domain within Fbox7 and PI31 · the same entry in another collection · chain A against A, TM-score 1.00
Q92530 · AlphaFold monomer V2.0 prediction for proteasome inhibitor PI31 subunit (Q92530) · a predicted model of the same protein · chain B 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 Q92530
Elsewhere: RCSB PDB 2VT8 · PDBe 2VT8 · UniProt Q92530

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