MolNFT v1 · #76842 · protein

CED-2

3QWY · Cell death abnormality protein 2: “CED-2”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.35). MolNFT v1 #76842 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3QWY
Type: protein
Length: 340 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell death abnormality protein 2
UniProt: Q9NHC3
Ligands: SO4
Pockets: 4 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cell death abnormality protein 2	protein	170	17% helix, 34% strand	Q9NHC3

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · chains B

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

Pockets

4 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	106	0.35	0.73	22	empty
2	66	0.33	0.76	15	empty
3	67	0.31	0.74	16	empty
4	50	0.27	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 371 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3QWY · CED-2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9NHC3 · AlphaFold monomer V2.0 prediction for cell death abnormality protein 2 (Q9NHC3) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 Q9NHC3
Elsewhere: RCSB PDB 3QWY · PDBe 3QWY · UniProt Q9NHC3

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