› 7urf

Electron Microscopy
2.8Å resolution

Human HHAT H379C in complex with SHH N-terminal peptide

Released:
DOI: 10.2210/pdb7urf/pdb
PDB entry 7urf coloured by chain, front view.
PDB entry 7urf coloured by chain, side view.
PDB entry 7urf 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-26711

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-226222 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Protein-cysteine N-palmitoyltransferase HHAT Chain: A
Molecule details ›
Chain: A
Length: 500 amino acids
Theoretical weight: 58.21 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q5VTY9 (Residues: 1-493; Coverage: 100%)
Gene names: HHAT, MART2, SKI1
Sequence domains: MBOAT, membrane-bound O-acyltransferase family
Sonic hedgehog protein N-product Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 694 Da
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q15465 (Residues: 24-30; Coverage: 2%)
Gene name: SHH
3H02 heavy chain Chain: O
3H02 light chain Chain: P

Ligands and Environments

3 bound ligands:
Ligand HEM 1 x HEM
Ligand PKZ 2 x PKZ
Ligand AJP 5 x AJP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 2.8Å
Relevant EMDB volumes: EMD-26711
Expression system: Homo sapiens

Quick links

Citations

11 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)
10 more

2 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)
1 more