MolNFT v1 · #45538 · protein
DDFLN5+110
2N62 · Gelation factor, secretion monitor chimera: “DDFLN5+110”. Solution nmr, 1 pocket (best druggability 0.48). MolNFT v1 #45538 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2N62
- Type
- protein
- Length
- 221 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gelation factor, secretion monitor chimera
- UniProt
- P13466, P62395
- Pockets
- 1 · best druggability 0.48
Structure
solution nmr · 1 distinct chain · 3% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Gelation factor, secretion monitor chimera | protein | 221 | 3% helix, 25% strand | P13466, P62395 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.48 | 0.78 | 24 | empty |
Compared structures
- 2N62 · ddFLN5+110 · the same entry in another collection · chain L against L, TM-score 1.00
- P13466 · AlphaFold monomer V2.0 prediction for gelation factor (P13466) · a predicted model of the same protein · chain L against A, TM-score 0.53
- P62395 · AlphaFold monomer V2.0 prediction for secretion monitor (P62395) · a predicted model of the same protein · chain L against A, TM-score 0.18
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 P13466
- Every structure of UniProt P62395
- Elsewhere: RCSB PDB 2N62 · PDBe 2N62 · UniProt P13466 · UniProt P62395
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