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Structure of Caspase-8/cFLIP death effector domain assembly

Analyse Structure of Caspase-8/cFLIP death effector domain assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8YM6
Type: protein
Length: 2,270 residues
Chains: 13
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.3
Source: Homo sapiens
Molecule: Caspase-8 subunit p10; CASP8 and FADD-like apoptosis regulator subunit p43
UniProt: Q14790, O15519
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · resolution 3.3 · 10 distinct chains · 64% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A	Caspase-8 subunit p10	protein	179	63% helix, 1% strand	Q14790
B, D	Caspase-8 subunit p10	protein	181	62% helix, 1% strand	Q14790
H, O	CASP8 and FADD-like apoptosis regulator subunit p43	protein	175	63% helix, 1% strand	O15519
G	CASP8 and FADD-like apoptosis regulator subunit p43	protein	176	63% helix, 1% strand	O15519
F	CASP8 and FADD-like apoptosis regulator subunit p43	protein	169	66% helix, 1% strand	O15519
K	CASP8 and FADD-like apoptosis regulator subunit p43	protein	169	65% helix, 1% strand	O15519
I	CASP8 and FADD-like apoptosis regulator subunit p43	protein	172	65% helix, 1% strand	O15519
J	CASP8 and FADD-like apoptosis regulator subunit p43	protein	173	66% helix, 1% strand	O15519
M	CASP8 and FADD-like apoptosis regulator subunit p43	protein	169	65% helix, 1% strand	O15519
N	CASP8 and FADD-like apoptosis regulator subunit p43	protein	172	64% helix, 1% strand	O15519

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	945	0.80	0.82	119	empty
2	1016	0.79	0.81	108	empty
3	740	0.78	0.82	70	empty
4	1016	0.75	0.78	81	empty
5	430	0.73	0.83	43	empty

Interfaces

29 interfaces between chains.

C–D · 937 Å² buried · 22 hydrogen bonds · protein-protein
A–H · 936 Å² buried · 13 hydrogen bonds · protein-protein
B–A · 901 Å² buried · 17 hydrogen bonds · protein-protein
C–B · 888 Å² buried · 17 hydrogen bonds · protein-protein
H–G · 857 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

Q14790 · AlphaFold monomer V2.0 prediction for caspase-8 (Q14790) · a predicted model of the same protein · chain C against A, TM-score 0.99
O15519 · AlphaFold monomer V2.0 prediction for CASP8 and fadd-like apoptosis regulator (O15519) · a predicted model of the same protein · chain M 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 Q14790
Every structure of UniProt O15519
Elsewhere: RCSB PDB 8YM6 · PDBe 8YM6 · UniProt Q14790 · UniProt O15519

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