MolNFT v1 · #99650 · protein

Crystal structure of ced-3

4M9R · Cell death protein 3: “Crystal structure of ced-3”. X-ray diffraction, 4 pockets (best druggability 0.69). MolNFT v1 #99650 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4M9R
Type: protein
Length: 479 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell death protein 3
EC: 3.4.22.-
UniProt: P42573
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell death protein 3 (EC 3.4.22.-)	protein	256	27% helix, 21% strand	P42573
B	Cell death protein 3 (EC 3.4.22.-)	protein	223	32% helix, 23% strand	P42573

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	240	0.69	0.86	29	empty
2	67	0.61	0.91	24	empty
3	56	0.31	0.76	12	empty
4	52	0.26	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 1685 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

4M9R · Crystal structure of CED-3 · the same entry in another collection · chain A against A, TM-score 1.00
P42573 · AlphaFold monomer V2.0 prediction for cell death protein 3 (P42573) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P42573
Elsewhere: RCSB PDB 4M9R · PDBe 4M9R · UniProt P42573

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