Research workbench
Cryo-EM structure of human TTYH3 in CA2+ and gdn
Analyse Cryo-EM structure of human TTYH3 in CA2+ and gdn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P5C
- Type
- protein
- Length
- 784 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tweety homolog 3
- UniProt
- Q9C0H2
- Ligands
- NAG
- Pockets
- 8 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 83% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein tweety homolog 3 | protein | 392 | 83% helix, 1% strand | Q9C0H2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 789 | 0.78 | 0.81 | 54 | empty |
| 2 | 770 | 0.78 | 0.81 | 52 | empty |
| 3 | 884 | 0.71 | 0.76 | 84 | empty |
| 4 | 132 | 0.52 | 0.81 | 17 | empty |
| 5 | 138 | 0.47 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2001 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 glycan, 4 disulfide (N-glycosylation, disulfide).
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 Q9C0H2
- Elsewhere: RCSB PDB 7P5C · PDBe 7P5C · UniProt Q9C0H2
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