MolNFT v1 · #114456 · protein

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

5BPZ · ANAPC5 protein: “Atomic-resolution structures of the APC/C subunits APC4 and the APC5 N-terminal domain”. X-ray diffraction, 1 pocket (best druggability 0.54). MolNFT v1 #114456 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5BPZ
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ANAPC5 protein
UniProt: Q0IH16
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ANAPC5 protein	protein	140	73% helix, 0% strand	Q0IH16

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.54	0.80	24	empty

Compared structures

5BPZ · 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

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 Q0IH16
Elsewhere: RCSB PDB 5BPZ · PDBe 5BPZ · UniProt Q0IH16

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