Research workbench

Crystal structure of full-length caspase-6 zymogen

Analyse Crystal structure of full-length caspase-6 zymogen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IYR
Type: protein
Length: 439 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Caspase-6
EC: 3.4.22.59
UniProt: P55212
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Caspase-6 (EC 3.4.22.59)	protein	248	27% helix, 26% strand	P55212
B	Caspase-6 (EC 3.4.22.59)	protein	191	34% helix, 22% strand	P55212

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	104	0.55	0.84	31	empty
2	111	0.50	0.80	25	empty
3	74	0.32	0.74	15	empty
4	73	0.31	0.73	20	empty

Interfaces

1 interface between chains.

A–B · 1346 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4IYR · Crystal structure of full-length caspase-6 zymogen · the same entry in another collection · chain A against A, TM-score 1.00
P55212 · AlphaFold monomer V2.0 prediction for caspase-6 (P55212) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P55212
Elsewhere: RCSB PDB 4IYR · PDBe 4IYR · UniProt P55212

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