Category
page 1Protein structural motifs
alpha helix
type of secondary structure
beta sheet
common motif of regular secondary structure in proteins; stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation
zinc finger
small structural protein motif found mostly in transcriptional genes

helix-turn-helix motif
200px|thumb|The λ repressor of bacteriophage lambda employs two helix-turn-helix motifs (left; green) to bind [[DNA (right; blue and red). The λ repressor protein in this image is a dimer.]]
structural motif
(in a chain-like biological molecule, such as a protein or nucleic acid) supersecondary structure, which also appears in a variety of other molecules
Leucine zipper
DNA-binding structural motif
basic helix-loop-helix transcription factor
transcription regulator protein
Rossmann fold
protein structural motif found in proteins that bind nucleotides
Collagen triple helix repeat
InterPro Repeat
pi helix
secondary protein structure
beta hairpin
secondary structure motif of proteins
310 helix
type of secondary structure
Zinc finger, RING-type
InterPro Domain
Walker motif
ATP-binding protein sequence motifs

turn
element of secondary structure in proteins where the polypeptide chain reverses its overall direction
Polyproline helix
Type of protein secondary structure
Transmembrane domain
membrane-spanning protein domain
Beta-sandwich
right|thumb|Illustration of the β-sandwich from Tenascin C (PDB entry: ).
Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology
triple helix
set of three congruent geometrical helices with the same axis
F-box protein
protein family
Alpha sheet
secondary protein structure
Beta bulge
localized disruption of the regular hydrogen bonding of a beta sheet
Chromogranin A/B/C
Granin (chromogranin and secretogranin) is a protein family of regulated secretory proteins ubiquitously found in the cores of amine and peptide hormone and neurotransmitter dense-core secretory vesicles.