Research workbench
Crystal structure of a TGF-beta ligand-receptor complex
Analyse Crystal structure of a TGF-beta ligand-receptor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QB4
- Type
- protein
- Length
- 388 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P43026, P36894
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 105 | — | P43026 |
| B | — | protein | 88 | — | P36894 |
| C | — | protein | 106 | — | P43026 |
| D | — | protein | 89 | — | P36894 |
Compared structures
- 3QB4 · Crystal structure of a TGF-beta ligand-receptor complex · the same entry in another collection · chain D against D, TM-score 1.00
- P43026 · AlphaFold monomer V2.0 prediction for GROWTH/DIFFERENTIATION factor 5 (P43026) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P36894 · AlphaFold monomer V2.0 prediction for bone morphogenetic protein receptor type-1A (P36894) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P43026
- Every structure of UniProt P36894
- Elsewhere: RCSB PDB 3QB4 · PDBe 3QB4 · UniProt P43026 · UniProt P36894
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