Evidence map›Paper›PMID 42024582›Full record

ArticleBioinformatics (Oxford, England)2026

StrucPTM: a database of structurally validated protein modifications and their conformational variation.

Seong-Gwang Jeon, Jejoong Yoo, Keehyoung Joo, Eunok Paek

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Article in Bioinformatics (Oxford, England), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

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4 authors.

Seong-Gwang JeonDepartment of Computer Science, Hanyang University, Seoul, 04763, Korea.
Jejoong YooSchool of Computational Sciences, Korea Institute for Advanced Study, Seoul, 02455, Korea.
Keehyoung JooCenter for Advanced Computation, Korea Institute for Advanced Study, Seoul, 02455, Korea.ORCID 0000-0002-4612-0927
Eunok PaekDepartment of Computer Science, Hanyang University, Seoul, 04763, Korea.ORCID 0000-0003-3655-9749

Funding

Institute of Information & communications Technology Planning & Evaluation (IITP)Korea government (MSIT) 2020-0-01373Korea government (MSIT) 2023-00220628
6 · The paper itself

Abstract

motivationPost-translational modifications (PTMs) alter functional states and interaction specificity largely through the conformational changes they impose on protein structure. However, most existing resources remain sequence-centric and cannot reveal how chemical modifications reshape 3D structures. To address this gap, we propose a structural database that systematically extracts and contextualizes modification sites within experimentally determined protein structures, providing a foundation for future studies of protein structure, function, and regulatory mechanisms.

resultsWe present StrucPTM, a database that extracts modified residues directly from the Protein Data Bank (PDB) structures using atom-level composition rules, substantially expanding coverage beyond annotation-dependent methods. Each validated PTM modification is mapped onto a UniProt entry. The database further characterizes residues using key structural descriptors-including secondary structure, relative solvent accessibility (RSA), and whether the PTM site lies at an interchain interface. All chains associated with the same UniProt ID are compared and grouped into homolog sets based on sequence identity. This emphasizes structural conservation among homologs, allowing PTM-induced conformational deviations to be distinguished from unrelated sequence divergence. AVAILABILITY AND IMPLEMENTATION: StrucPTM offers searchable access, interactive 3D visualization, and homolog-based structural comparison through its web interface: https://prix.hanyang.ac.kr/strucptm. The source code and datasets are permanently archived on Zenodo (DOI: 10.5281/zenodo.18939125) and are accessible via GitHub (https://github.com/HanyangBISLab/StrucPTM.git).

Indexed as

Databases, ProteinProtein Processing, Post-TranslationalProteinsProtein ConformationSoftwareProteins

Identifiers

PMID42024582
PMCPMC13138842

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.