Structure analysis

ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with inosine diphosphate ribose (IDPr)

X-ray diffraction
1.77Å resolution
Source organism: Latimeria chalumnae
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12975.45 Å2
Buried surface area: 1387.01 Å2
Dissociation area: 121.77 Å2
Dissociation energy (ΔGdiss): -0.42 kcal/mol
Dissociation entropy (TΔSdiss): 0.88 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-124772
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 13086.18 Å2
Buried surface area: 1299.19 Å2
Dissociation area: 104.24 Å2
Dissociation energy (ΔGdiss): -0.19 kcal/mol
Dissociation entropy (TΔSdiss): 0.81 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-124772

Macromolecules

Chains: A, B
Length: 350 amino acids
Theoretical weight: 38.29 KDa
Source organism: Latimeria chalumnae
Expression system: Escherichia coli
UniProt:
  • Canonical: H3BCW1 (Residues: 10-356; Coverage: 98%)
Gene names: adprhl2, adprs, arh3
Pfam: ADP-ribosylglycohydrolase
InterPro:
CATH: ADP-ribosylation/Crystallin J1

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