Research workbench

Atomic-resolution structures of the APC/C subunits APC4 and the APC5 N-terminal domain

Analyse Atomic-resolution structures of the APC/C subunits APC4 and the APC5 N-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BPW
Type: protein
Length: 659 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anaphase-promoting complex subunit 4
UniProt: Q9UJX5
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anaphase-promoting complex subunit 4	protein	659	30% helix, 30% strand	Q9UJX5

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	697	0.81	0.85	54	empty
2	536	0.69	0.78	46	empty
3	209	0.61	0.82	23	empty
4	96	0.60	0.87	20	empty
5	290	0.58	0.77	27	empty

Compared structures

5BPW · Atomic-resolution structures of the APC/C subunits Apc4 and the Apc5 N-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9UJX5 · AlphaFold monomer V2.0 prediction for anaphase-promoting complex subunit 4 (Q9UJX5) · a predicted model of the same protein · chain A 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 Q9UJX5
Elsewhere: RCSB PDB 5BPW · PDBe 5BPW · UniProt Q9UJX5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.