› 7nai

X-ray diffraction
1.74Å resolution

Crystal structure of the TIR domain from human SARM1 in complex with 3AD

Released:
DOI: 10.2210/pdb7nai/pdb
Model geometry
Fit model/data
PDB entry 7nai coloured by chain, front view.
PDB entry 7nai coloured by chain, side view.
PDB entry 7nai coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules.
Shi Y, Kerry PS, Nanson JD, Bosanac T, Sasaki Y, Krauss R, Saikot FK, Adams SE, Mosaiab T, Masic V, Mao X, Rose F, Vasquez E, Furrer M, Cunnea K, Brearley A, Gu W, Luo Z, Brillault L, Landsberg MJ, DiAntonio A, Kobe B, Milbrandt J, Hughes RO, Ve T
Mol Cell 82 1643-1659.e10 (2022)
PMID: 35334231

Function and Biology Details

Reaction catalysed: 
(1a) NAD(+) = cyclic ADP-ribose + nicotinamide
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180341 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(+) hydrolase SARM1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 144 amino acids
Theoretical weight: 16.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6SZW1 (Residues: 560-700; Coverage: 20%)
Gene names: KIAA0524, SAMD2, SARM, SARM1
Sequence domains: TIR domain

Ligands and Environments

1 bound ligand:
Ligand 1O4 2 x 1O4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21212
Unit cell:
a: 86.192Å b: 116.779Å c: 33.016Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Reactivity of Covalent Fragments and Their Role in Fragment Based Drug Discovery.
McAulay et al. (2022)
3 more

2 mentions without citation

Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules.
Shi et al. (2022)
1 more