Research workbench
Structure of filamin a immunoglobulin-like repeat 10 from homo sapiens
Analyse Structure of filamin a immunoglobulin-like repeat 10 from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RGH
- Type
- protein
- Length
- 195 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Filamin-a
- UniProt
- P21333
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Filamin-a | protein | 98 | 6% helix, 50% strand | P21333 |
| B | Filamin-a | protein | 97 | 6% helix, 51% strand | P21333 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.70 | 0.96 | 17 | empty |
| 2 | 125 | 0.40 | 0.75 | 32 | empty |
| 3 | 103 | 0.39 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 562 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (artifact).
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 P21333
- Elsewhere: RCSB PDB 3RGH · PDBe 3RGH · UniProt P21333
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