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Structure of parkin-S223P E3 ligase

Analyse Structure of parkin-S223P E3 ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I1F
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase parkin
EC: 6.3.2.-
UniProt: O60260
Ligands: ZN, BA
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase parkin (EC 6.3.2.-)	protein	306	18% helix, 25% strand	O60260

Ligands and binding sites

ZN · Zinc ion · metal · 8 copies · chains A
BA · Barium ion · metal · chains A

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

Pockets

4 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	239	0.56	0.78	19	empty
2	72	0.41	0.79	18	empty
3	54	0.27	0.74	15	empty
4	53	0.27	0.73	14	empty

Compared structures

4I1F · Structure of Parkin-S223P E3 ligase · the same entry in another collection · chain A against A, TM-score 1.00
O60260 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase parkin (O60260) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 O60260
Elsewhere: RCSB PDB 4I1F · PDBe 4I1F · UniProt O60260

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