MolNFT v1 · #118864 · protein

TRIM32 RING

5FEY · E3 ubiquitin-protein ligase TRIM32: “TRIM32 RING”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.49). MolNFT v1 #118864 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5FEY
Type: protein
Length: 157 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase TRIM32
EC: 6.3.2.-
UniProt: Q13049
Ligands: ZN
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase TRIM32 (EC 6.3.2.-)	protein	78	24% helix, 18% strand	Q13049
B	E3 ubiquitin-protein ligase TRIM32 (EC 6.3.2.-)	protein	79	32% helix, 15% strand	Q13049

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.49	0.81	16	empty
2	100	0.49	0.81	16	empty
3	59	0.39	0.80	12	empty

Interfaces

1 interface between chains.

A–B · 1064 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5FEY · TRIM32 RING · the same entry in another collection · chain A against A, TM-score 1.00
Q13049 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM32 (Q13049) · a predicted model of the same protein · chain B against A, TM-score 0.93

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 Q13049
Elsewhere: RCSB PDB 5FEY · PDBe 5FEY · UniProt Q13049

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