Research workbench
Crystal structure of tradd death domain glcnacylated by epec effector nleb
Analyse Crystal structure of tradd death domain glcnacylated by epec effector nleb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AC0
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor necrosis factor receptor type 1-associated death domain protein
- UniProt
- Q15628
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor necrosis factor receptor type 1-associated death domain protein | protein | 115 | 63% helix, 9% strand | Q15628 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 glycan (glycosylation).
Compared structures
- 6AC0 · Crystal structure of TRADD death domain GlcNAcylated by EPEC effector NleB · the same entry in another collection · chain A against A, TM-score 1.00
- Q15628 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor type 1-associated… · 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 Q15628
- Elsewhere: RCSB PDB 6AC0 · PDBe 6AC0 · UniProt Q15628
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