Research workbench
Cryo-EM structure of human PTCH1
Analyse Cryo-EM structure of human PTCH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DMB
- Type
- protein
- Length
- 990 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein patched homolog 1
- UniProt
- Q13635
- Ligands
- Y01, NAG
- Pockets
- 15 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 53% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein patched homolog 1 | protein | 990 | 53% helix, 5% strand | Q13635 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 2 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 780 | 0.88 | 0.90 | 95 | empty |
| 2 | 242 | 0.79 | 0.91 | 26 | Y01 |
| 3 | 221 | 0.62 | 0.81 | 44 | empty |
| 4 | 204 | 0.58 | 0.80 | 29 | empty |
| 5 | 262 | 0.56 | 0.77 | 22 | empty |
Modifications
Observed in the structure: 6 glycan, 3 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 Q13635
- Elsewhere: RCSB PDB 6DMB · PDBe 6DMB · UniProt Q13635
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