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. 2024 Mar 12;2024:baae009. doi: 10.1093/database/baae009

Table 1.

The table shows a list of databases that can be consulted to retrieve information and references on experimental studies in proteins

Resource Description URL
Protein Data Bank in Europe (PDBe) (28) X-ray crystallography, nuclear magnetic resonance (NMR)-related methods, and electron microscopy protein structures https://www.ebi.ac.uk/pdbe
Biological Magnetic Resonance Bank (BMRB) (29) Spectral and quantitative data derived from NMR spectroscopy http://www.bmrb.wisc.edu
Small Angle Scattering Biological Data Bank (SASBDB) (30) Small-angle x-ray scattering (SAXS) and small-angle neutron scattering experiments https://www.sasbdb.org/
Electron Microscopy Data Bank (EMDB) (31) Electron Microscopy Data Bank for electron cryo-microscopy, single-particle analysis, electron tomography, and electron crystallography https://www.ebi.ac.uk/pdbe/emdb/
Protein Circular Dichroism Data Bank (PCDDB) (32) Circular dichroism (CD) and synchrotron radiation CD (SRCD) spectral data and their associated experimental metadata http://pcddb.cryst.bbk.ac.uk/home.php
PhaSePro (33) Manually curated resource of proteins driving liquid–liquid phase separation (LLPS) https://phasepro.elte.hu/
AmyPro Validated amyloid precursor proteins and their amyloidogenic sequence regions https://amypro.net/#/
Eukaryotic Linear Motif (ELM) (34) Curated database of short linear motifs in eukaryotes http://elm.eu.org/searchdb.html
UniProt (35) Resource of protein sequence and functional information https://www.uniprot.org/
MobiDB (36) Database of protein disorder and mobility annotations https://mobidb.bio.unipd.it/

Some of these resources pertain to techniques used in structural biology and are linked to scientific articles, while others, like MobiDB, serve as sources to extract information about the possible disorder state of a protein, which can be either predicted or curated. Indeed, in the last version of DisProt, another track specifically highlights the disordered regions derived from the missing residues of the PDB, as calculated by MobiDB (consensus trace)