MolNFT v1 · #147068 · protein
Structure of 2:1 human PTCH1-shh-N complex
6E1H: “Structure of 2:1 human PTCH1-shh-N complex”. Electron microscopy, 3 ligands (PLM, CA, ZN). MolNFT v1 #147068 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6E1H
- Type
- protein
- Length
- 2,120 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13635, Q15465
- Ligands
- PLM, CA, ZN
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 978 | — | Q13635 |
| C | — | protein | 164 | — | Q15465 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · chains A, C
- CA · Calcium ion · metal · 2 copies · chains C
- ZN · Zinc ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6E1H · Structure of 2:1 human Ptch1-Shh-N complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q13635 · AlphaFold monomer V2.0 prediction for protein patched homolog 1 (Q13635) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q15465 · AlphaFold monomer V2.0 prediction for sonic hedgehog protein (Q15465) · a predicted model of the same protein · chain C against A, TM-score 0.91
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
- Every structure of UniProt Q15465
- Elsewhere: RCSB PDB 6E1H · PDBe 6E1H · UniProt Q13635 · UniProt Q15465
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