Research workbench
Solution structure of disulfide bond mutaion of the core domain of fibroblast growth factor 21 (FGF21)
Analyse Solution structure of disulfide bond mutaion of the core domain of fibroblast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M6F
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor 21
- UniProt
- Q9NSA1
- Pockets
- 1 · best druggability 0.52
Structure
solution nmr · 1 distinct chain · 5% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor 21 | protein | 129 | 5% helix, 41% strand | Q9NSA1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.52 | 0.75 | 23 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6M6F · Solution structure of disulfide bond mutaion of the core domain of Fibroblast growth… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NSA1 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 21 (Q9NSA1) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q9NSA1
- Elsewhere: RCSB PDB 6M6F · PDBe 6M6F · UniProt Q9NSA1
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