Research workbench
Moesin ferm domain bound to EBP50 C-terminal peptide
Analyse Moesin ferm domain bound to EBP50 C-terminal peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SGH
- Type
- protein
- Length
- 332 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Moesin; Ezrin-radixin-moesin binding phosphoprotein 50
- UniProt
- P26038, O14745
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Moesin | protein | 294 | 31% helix, 22% strand | P26038 |
| B | Ezrin-radixin-moesin binding phosphoprotein 50 | protein | 38 | 0% helix, 0% strand | O14745 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.64 | 0.76 | 49 | empty |
| 2 | 176 | 0.57 | 0.80 | 31 | empty |
| 3 | 76 | 0.52 | 0.84 | 23 | empty |
| 4 | 101 | 0.50 | 0.82 | 28 | empty |
| 5 | 197 | 0.49 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 563 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1SGH · Moesin FERM domain bound to EBP50 C-terminal peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P26038 · AlphaFold monomer V2.0 prediction for moesin (P26038) · a predicted model of the same protein · chain A against A, TM-score 0.97
- O14745 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF1… · a predicted model of the same protein · chain B against A, TM-score 0.31
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 P26038
- Every structure of UniProt O14745
- Elsewhere: RCSB PDB 1SGH · PDBe 1SGH · UniProt P26038 · UniProt O14745
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