6o0t

X-ray diffraction
2.8Å resolution

Crystal structure of selenomethionine labelled tandem SAM domains (L446M:L505M:L523M mutant) from human SARM1

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180347 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(+) hydrolase SARM1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 177 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6SZW1 (Residues: 409-561; Coverage: 21%)
Gene names: KIAA0524, SAMD2, SARM, SARM1
Sequence domains: SAM domain (Sterile alpha motif)

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Unit cell:
a: 94.24Å b: 154.08Å c: 120.995Å
α: 90° β: 94.55° γ: 90°
R-values:
R R work R free
0.202 0.2 0.238
Expression system: Escherichia coli