› 7urc

Electron Microscopy
3.14Å resolution

Human PORCN in complex with LGK974

Released:
DOI: 10.2210/pdb7urc/pdb
PDB entry 7urc coloured by chain, front view.
PDB entry 7urc coloured by chain, side view.
PDB entry 7urc coloured by chain, top view.
Source organisms:
Primary publication:
Mechanisms and inhibition of Porcupine-mediated Wnt acylation.
Liu Y, Qi X, Donnelly L, Elghobashi-Meinhardt N, Long T, Zhou RW, Sun Y, Wang B, Li X
Nature 607 816-822 (2022)
PMID: 35831507
Related structures: EMD-26708

Function and Biology Details

Reaction catalysed: 
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-226356 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein-serine O-palmitoleoyltransferase porcupine Chain: A
Molecule details ›
Chain: A
Length: 464 amino acids
Theoretical weight: 52.82 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9H237 (Residues: 2-461; Coverage: 99%)
  • Best match: Q9H237-2 (Residues: 2-456)
Gene names: MG61, PORC, PORCN, PPN
Sequence domains: MBOAT, membrane-bound O-acyltransferase family
2C11 light chain Chain: L
Molecule details ›
Chain: L
Length: 234 amino acids
Theoretical weight: 25.67 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
2C11 heavy chain Chain: H

Ligands and Environments

4 bound ligands:
Ligand O50 1 x O50
Ligand CLR 9 x CLR
Ligand AJP 1 x AJP
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.14Å
Relevant EMDB volumes: EMD-26708
Expression system: Homo sapiens

Quick links

Citations

15 review citations

Wnt/β-Catenin Signaling and Resistance to Immune Checkpoint Inhibitors: From Non-Small-Cell Lung Cancer to Other Cancers.
Muto et al. (2023)
14 more

3 mentions without citation

A rising tide lifts all MBOATs: recent progress in structural and functional understanding of membrane bound O-acyltransferases.
Pierce et al. (2023)
2 more