MolNFT v1 · #5035 · protein
Structure of isolated ferm domain and first long helix of moesin
1E5W: “Structure of isolated ferm domain and first long helix of moesin”. X-ray diffraction, 5 pockets (best druggability 0.68). MolNFT v1 #5035 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1E5W
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Moesin
- UniProt
- P26038
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Moesin | protein | 346 | 42% helix, 21% strand | P26038 |
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 | 641 | 0.68 | 0.77 | 52 | empty |
| 2 | 155 | 0.55 | 0.81 | 16 | empty |
| 3 | 172 | 0.48 | 0.76 | 20 | empty |
| 4 | 113 | 0.44 | 0.77 | 28 | empty |
| 5 | 114 | 0.40 | 0.76 | 18 | empty |
Compared structures
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
- Elsewhere: RCSB PDB 1E5W · PDBe 1E5W · UniProt P26038
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