Research workbench
Crystal structure of human TLE1 Q-domain residues 20-156
Analyse Crystal structure of human TLE1 Q-domain residues 20-156 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OM3
- Type
- protein
- Length
- 468 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q04724
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 117 | — | Q04724 |
| B | — | protein | 112 | — | Q04724 |
| D | — | protein | 122 | — | Q04724 |
Compared structures
- 4OM3 · Crystal structure of human TLE1 Q-domain residues 20-156 · the same entry in another collection · chain A against A, 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 Q04724
- Elsewhere: RCSB PDB 4OM3 · PDBe 4OM3 · UniProt Q04724
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