Research workbench
Extracellular domain of type II transforming growth factor beta receptor in complex with ndsb-201
Analyse Extracellular domain of type II transforming growth factor beta receptor in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P7U
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TGF-beta receptor type-2
- EC
- 2.7.11.30
- UniProt
- P37173
- Ligands
- 1PS
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TGF-beta receptor type-2 (EC 2.7.11.30) | protein | 102 | 3% helix, 45% strand | P37173 |
Ligands and binding sites
- 1PS · 3-pyridinium-1-ylpropane-1-sulfonate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 4P7U · Extracellular domain of type II Transforming Growth Factor Beta receptor in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P37173 · AlphaFold monomer V2.0 prediction for TGF-beta receptor type-2 (P37173) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P37173
- Elsewhere: RCSB PDB 4P7U · PDBe 4P7U · UniProt P37173
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