Research workbench
TGF-beta receptor type 2 kinase domain (E431A,R433A,E485A,K488A,R493A, R495A) in complex with amppnp
Analyse TGF-beta receptor type 2 kinase domain (E431A,R433A,E485A,K488A,R493A, R495A)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E92
- Type
- protein
- Length
- 298 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
- ANP, MG
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TGF-beta receptor type-2 (EC 2.7.11.30) | protein | 298 | 40% helix, 19% strand | P37173 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.68 | 0.83 | 36 | ANP, MG |
| 2 | 118 | 0.61 | 0.86 | 27 | empty |
| 3 | 89 | 0.37 | 0.75 | 24 | empty |
| 4 | 63 | 0.31 | 0.75 | 12 | empty |
| 5 | 52 | 0.28 | 0.75 | 15 | empty |
Compared structures
- 5E92 · TGF-beta receptor type 2 kinase domain (E431A,R433A,E485A,K488A,R493A,R495A) in complex… · 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 0.99
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 P37173
- Elsewhere: RCSB PDB 5E92 · PDBe 5E92 · UniProt P37173
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