MolNFT v1 · #154002 · protein

Hect domain of AREL1

6JX5 · Apoptosis-resistant E3 ubiquitin protein ligase 1: “Hect domain of AREL1”. X-ray diffraction, 19 pockets (best druggability 0.55). MolNFT v1 #154002 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6JX5
Type: protein
Length: 1,134 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apoptosis-resistant E3 ubiquitin protein ligase 1
EC: 2.3.2.26
UniProt: O15033
Pockets: 19 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A, B	Apoptosis-resistant E3 ubiquitin protein ligase 1 (EC 2.3.2.26)	protein	378	50% helix, 13% strand	O15033

Pockets

19 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.55	0.88	21	empty
2	219	0.54	0.78	29	empty
3	60	0.52	0.88	21	empty
4	137	0.50	0.79	19	empty
5	270	0.49	0.74	33	empty

Interfaces

2 interfaces between chains.

A–B · 1048 Å² buried · 4 hydrogen bonds · protein-protein
C–A · 119 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6JX5 · Hect domain of AREL1 · the same entry in another collection · chain C against C, TM-score 1.00
O15033 · AlphaFold monomer V2.0 prediction for apoptosis-resistant E3 ubiquitin protein ligase 1… · a predicted model of the same protein · chain C 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 O15033
Elsewhere: RCSB PDB 6JX5 · PDBe 6JX5 · UniProt O15033

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