Research workbench
Crystal structure of the FAS/FADD death domain complex
Analyse Crystal structure of the FAS/FADD death domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EZQ
- Type
- protein
- Length
- 1,712 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25445, Q13158
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | — | protein | 115 | — | P25445 |
| B, D, F, H, J, L, N, P | — | protein | 99 | — | Q13158 |
Compared structures
- 3EZQ · Crystal Structure of the Fas/FADD Death Domain Complex · the same entry in another collection · chain J against J, TM-score 1.00
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 P25445
- Every structure of UniProt Q13158
- Elsewhere: RCSB PDB 3EZQ · PDBe 3EZQ · UniProt P25445 · UniProt Q13158
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