Research workbench

alternative p35-caspase-8 complex

Analyse alternative p35-caspase-8 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FUN
Type: protein
Length: 1,070 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3
Source: Autographa californica nucleopolyhedrovirus; Homo sapiens
Molecule: Early 35 kDa protein; caspase-8
UniProt: P08160, Q14790
Pockets: 12 · best druggability 0.65

Structure

x-ray diffraction · resolution 3 · 3 distinct chains · 25% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Early 35 kDa protein	protein	293	16% helix, 41% strand	P08160
B	caspase-8	protein	243	30% helix, 19% strand	Q14790
D	caspase-8	protein	241	30% helix, 17% strand	Q14790

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	254	0.65	0.82	31	empty
2	252	0.64	0.82	26	empty
3	330	0.57	0.76	40	empty
4	85	0.51	0.83	19	empty
5	261	0.49	0.74	35	empty

Interfaces

2 interfaces between chains.

C–D · 1013 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 1000 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2FUN · Alternative P35-caspase-8 complex · the same entry in another collection · chain A against A, TM-score 1.00
Q14790 · AlphaFold monomer V2.0 prediction for caspase-8 (Q14790) · a predicted model of the same protein · chain B 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 P08160
Every structure of UniProt Q14790
Elsewhere: RCSB PDB 2FUN · PDBe 2FUN · UniProt P08160 · UniProt Q14790

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