Research workbench
Solution structure of human fibrillin-1 EGF2-EGF3-HYBRID1-CBEGF1 four domain fragment
Analyse Solution structure of human fibrillin-1 EGF2-EGF3-HYBRID1-CBEGF1 four domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MS9
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibrillin-1
- UniProt
- P35555
- Ligands
- CA
- Pockets
- 2 · best druggability 0.42
Structure
solution nmr · 1 distinct chain · 6% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibrillin-1 | protein | 177 | 6% helix, 28% strand | P35555 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.42 | 0.83 | 15 | empty |
| 2 | 80 | 0.29 | 0.72 | 15 | empty |
Modifications
Observed in the structure: 13 disulfide (disulfide).
Compared structures
- 5MS9 · Solution structure of Human Fibrillin-1 EGF2-EGF3-Hybrid1-cbEGF1 four domain fragment · the same entry in another collection · chain A against A, TM-score 1.00
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 P35555
- Elsewhere: RCSB PDB 5MS9 · PDBe 5MS9 · UniProt P35555
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.