Navigation

The app is organized in four tabs:

• Main tab: Browse and filter proteins in the dataset. Select a protein and a region to explore.
• Viewer tab: Visualize the selected protein in 3D and explore its sequence features interactively.
• Help tab: Usage instructions, contact information, and data downloads.
• About tab: Dataset construction details, app information, and citation.

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3D Structure Viewer

The 3D viewer displays AlphaFold models and experimental PDB structures for the selected protein.

• Use the Viewer Commands panel to toggle individual models on/off.
• Click on a region or PFAM domain in the sequence track to highlight it in the 3D structure.
• The highlighted region will be colored according to its track color.
• Use the mouse to rotate (left click + drag), zoom (scroll), and pan (right click + drag) the structure.

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1D Sequence & Feature Viewer

The sequence track displays the following layers from bottom to top:

• Sequence: Each amino acid is shown as a single letter at its UniProt position.
• pLDDT: AlphaFold per-residue confidence score, colored by the official AF colorscale:
  • ■ Very High (>90)
  • ■ High (70–90)
  • ■ Low (50–70)
  • ■ Very Low (<50)
• Regions (per PDB chain): Structural regions annotated per chain, color coded by type:
  • ■ Domain
  • ■ IDL — Independent Domain Linker
  • ■ DDL — Dependent Domain Linker
  • ■ Loops
• Disprot Linkers: DisProt-annotated linker regions, shown in dark red , one track per region.
• PFAM Domains: Pfam domain annotations, one color per domain name.

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Interactivity

• Click any region, Disprot linker, or PFAM domain in the track to highlight it in the 3D viewer and display its details in the Region Details panel.
• Hover over any element in the track to see a tooltip with coordinates and identifiers.
• Use the plotly toolbar (top right of the track) to zoom, pan, or reset the view .

Parameter	Definition	Source
FCR	Fraction of charged residues, between 0 and 1. FCR = f+ + f-	localCIDER
NCPR	Net charge per residue, between -1 and 1. NCPR = f+ - f-	localCIDER
Fraction of positive residues ( F+ )	F+ = F[K] + F[R]	localCIDER
Fraction of negative residues ( F- )	F- = F[D] + F[E]	localCIDER
Fraction of polar residues	F[S] + F[T] + F[N] + F[Q] + F[H] + F[G]	localCIDER
Fraction of proline residues	F[P]	localCIDER
Fraction of aliphatic residues	F[I] + F[L] + F[V] + F[M]	localCIDER
Fraction of aromatic residues	F[F] + F[Y] + F[W]	localCIDER
Fraction of expansion promoting residues	F[E] + F[D] + F[R] + F[K] + F[P]	localCIDER
Fraction of disorder promoting residues	F[T] + F[A] + F[G] + F[R] + F[D] + F[H] + F[Q] + F[K] + F[S] + F[E] + F[P]	localCIDER
Hydrophobicity	Mean hydrophobicity scaled from 0 to 9, calculated from the Kyte-Doolittle hydrophobicity scale.	SPARROW
SCD	Sequence charge decoration; captures the linear distribution of charged residues.	SPARROW
SHD	Sequence hydropathy decoration; captures the linear distribution of hydrophobicity.	SPARROW
Omega	Patterning between charged/proline residues and all other residues. A value of -1 means that the parameter cannot be calculated because of sequence composition.	localCIDER
Kappa	Patterning between positive and negative charged residues. A value of -1 means that the parameter cannot be calculated because of sequence composition.	SPARROW
End_to_end_distance	Predicted average distance between the termini in the ensemble. This is the scaled end-to-end distance.	SPARROW
Radius_of_gyration_scaled	Predicted average distance to the center of mass of the ensemble. This is the scaled radius of gyration.	SPARROW
Asphericity	Predicted deviation from a perfect, symmetrical ensemble.	SPARROW
Predicted Prefactor (rho0) and scaling exponent (nu)	Polymer laws: Rg = rho0 * N^nu . The prefactor depends on the details of the monomer and bond geometry. The scaling exponent depends on the dimensions of the chain, with a value of 3/5 for the expanded coil state.	SPARROW
Missing Percentage and Missing length	Missing residues in the PDB-chain.	Experimental

Download the full dataset files below. These files contain the complete data used to build this database, independent of any filter applied in the app.

Raw Data Files

Data with Details

For questions, bug reports, or feedback about the database or the app, please reach out to us at:

The DLD dataset identifies Independent Domain Linkers (IDLs) by extracting high-quality domain annotations from SCOP2, filtering for multi-domain proteins, and refining linker regions using DSSP-based secondary structure analysis.

A two-step smoothing process helps distinguish 1,640 IDLs and 647 Dependent Domain Linkers (DDLs), alongside other protein regions. The dataset is mapped to UniProt, providing a comprehensive resource for studying disordered flexible linkers and enhancing computational predictions.

* Equal contribution