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Structural insights into the catalytic mechanism of CD38: Evidence for a conformationally flexible covalent enzyme-substrate complex.

X-ray diffraction
1.51Å resolution
PDB entry 3gc6 coloured by chain, front view.
PDB entry 3gc6 coloured by chain, side view.
PDB entry 3gc6 coloured by chain, top view.
Source organism: Bos taurus
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
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Multimeric state: homo dimer
Accessible surface area: 22990.39 Å2
Buried surface area: 3177.5 Å2
Dissociation area: 647.66 Å2
Dissociation energy (ΔGdiss): 4.53 kcal/mol
Dissociation entropy (TΔSdiss): 12.5 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-193579
Assembly 2
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Assembly Name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
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Multimeric state: homo dimer
Accessible surface area: 22664.3 Å2
Buried surface area: 3503.59 Å2
Dissociation area: 810.7 Å2
Dissociation energy (ΔGdiss): -5.5 kcal/mol
Dissociation entropy (TΔSdiss): 12.77 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-193579

Macromolecules

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Chains: A, B
Length: 247 amino acids
Theoretical weight: 28.3 KDa
Source organism: Bos taurus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9TTF5 (Residues: 32-278; Coverage: 98%)
Gene name: CD38
Pfam: ADP-ribosyl cyclase
InterPro: ADP-ribosyl cyclase (CD38/157)
CATH:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase in PDB entry 3gc6, assembly 1, front view.
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase in PDB entry 3gc6, assembly 1, side view.
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase in PDB entry 3gc6, assembly 1, top view.
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