Research workbench
Human porcn in complex with palmitoleoylated WNT3A peptide
Analyse Human porcn in complex with palmitoleoylated WNT3A peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7URE
- Type
- protein
- Length
- 678 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9H237, P56704
- Ligands
- AJP, PAM, ZN
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 432 | — | Q9H237 |
| L | — | protein | 107 | — | — |
| H | — | protein | 119 | — | — |
| B | — | protein | 20 | — | P56704 |
Ligands and binding sites
- AJP · Digitonin · ligand · chains A, H
- PAM · Palmitoleic acid · ligand · chains A, B
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7URE · Human PORCN in complex with palmitoleoylated WNT3A peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H237 · AlphaFold monomer V2.0 prediction for protein-serine O-palmitoleoyltransferase porcupine… · a predicted model of the same protein · chain A against A, TM-score 0.98
- P56704 · AlphaFold monomer V2.0 prediction for protein wnt-3A (P56704) · a predicted model of the same protein · chain B against A, TM-score 0.41
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 Q9H237
- Every structure of UniProt P56704
- Elsewhere: RCSB PDB 7URE · PDBe 7URE · UniProt Q9H237 · UniProt P56704
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.