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Crystal structure of human STARD10
Analyse Crystal structure of human STARD10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SER
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Start domain-containing protein 10
- UniProt
- Q9Y365
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Start domain-containing protein 10 | protein | 245 | 27% helix, 36% strand | Q9Y365 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
- PGE · Triethylene glycol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 766 | 0.83 | 0.86 | 56 | PEG, PGE |
| 2 | 156 | 0.58 | 0.82 | 21 | PEG |
| 3 | 62 | 0.39 | 0.80 | 19 | 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 Q9Y365
- Elsewhere: RCSB PDB 6SER · PDBe 6SER · UniProt Q9Y365
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