› 7q1u

Electron Microscopy
2.7Å resolution

Structure of Hedgehog acyltransferase (HHAT) in complex with megabody 177 bound to non-hydrolysable palmitoyl-CoA (Composite Map)

Released:
DOI: 10.2210/pdb7q1u/pdb
PDB entry 7q1u coloured by chain, front view.
PDB entry 7q1u coloured by chain, side view.
PDB entry 7q1u coloured by chain, top view.
Source organisms:
Primary publication:
Structure, mechanism, and inhibition of Hedgehog acyltransferase.
Coupland CE, Andrei SA, Ansell TB, Carrique L, Kumar P, Sefer L, Schwab RA, Byrne EFX, Pardon E, Steyaert J, Magee AI, Lanyon-Hogg T, Sansom MSP, Tate EW, Siebold C
Mol Cell 81 5025-5038.e10 (2021)
PMID: 34890564
Related structures: EMD-13764

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154830 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein-cysteine N-palmitoyltransferase HHAT Chain: A
Molecule details ›
Chain: A
Length: 503 amino acids
Theoretical weight: 58.57 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
Glucosidase YgjK Chain: B
Molecule details ›
Chain: B
Length: 919 amino acids
Theoretical weight: 102.6 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P42592 (Residues: 22-484; Coverage: 61%)
Gene names: JW3051, b3080, ygjK
Sequence domains:

Ligands and Environments

5 bound ligands:
Ligand CLR 1 x CLR
Ligand HEM 1 x HEM
Ligand HD6 1 x HD6
Ligand MG 1 x MG
Ligand PLM 2 x PLM
1 modified residue:
Ligand P1L 1 x P1L

Experiments and Validation Details

Entry percentile scores
Resolution: 2.7Å
Relevant EMDB volumes: EMD-13764
Expression systems:
  • Homo sapiens
  • Escherichia coli

Quick links

Citations

5 review citations

Emerging roles of protein palmitoylation and its modifying enzymes in cancer cell signal transduction and cancer therapy.
Liu et al. (2022)
4 more

4 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)
3 more