Protein Structure: uses and methods
View structures, annotate residues, and perform Cα rigid body overlays.
Applicable scope and calculation boundary
PDB/mmCIF first model; alignment requires equal length according to Cα order, no sequence alignment is performed. The pockets are user-given residues and no binding sites are predicted.
model and reference method
Kabsch least squares rigid body superposition; Biopython structure analysis.
model version: 1.0.0. The results are used for scientific research, exploration and teaching, please interpret according to the model conditions.
input parameters
- reference structure
- example is a synthetic Cα helix and is for demonstration purposes only.
- Structure to be stacked (optional)
- same length Cα structure.
- marks the residue number
- comma separated; match all chains by residue number.
How to use
- Load the example or enter data that matches the field description.
- Confirm units and models, run calculations and check diagnostics.
- Export charts, tables or results packages and record model versions.
tools in the same field
are free and open; free sponsorship does not affect tool permissions. All functions of Read scientific methods and data explanations 。