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9VLF

Structural studies on the conformation changes induced by ligand binding in an Adenine phosphoribosyltransferase (FnAPRT) from Fusobacterium nucleatum

Summary for 9VLF
Entry DOI10.2210/pdb9vlf/pdb
DescriptorAdenine phosphoribosyltransferase, PHOSPHATE ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
Functional Keywordsfusobacterium nucleatum, adenine phosphoribosyltransferase, ligand binding, transferase
Biological sourceFusobacterium nucleatum
Total number of polymer chains1
Total formula weight19375.19
Authors
Kim, B.,Hwang, J.,Do, H.,Lee, J.H. (deposition date: 2025-06-25, release date: 2026-02-11)
Primary citationKim, B.,Hwang, J.,Do, H.,Shim, Y.S.,Lee, J.H.
Structural Insights into Ligand-Induced Conformational Changes in Adenine Phosphoribosyl Transferase from Fusobacterium nucleatum.
Protein Pept.Lett., 2026
Cited by
PubMed Abstract: Adenine phosphoribosyltransferase (APRT) is an enzyme that facilitates adenosine monophosphate (AMP) biosynthesis by transferring a phosphoribosyl group to adenine using phosphoribosyl pyrophosphate as a donor. While the human enzyme is well characterized, structural insights into bacterial APRTs remain limited. is associated with periodontal disease, yet its APRT enzyme (FnAPRT) has not been structurally investigated.
PubMed: 41588988
DOI: 10.2174/0109298665403166251021110505
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.61 Å)
Structure validation

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PDB entries from 2026-02-11

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