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Structure of FS1, the heparin-binding domain of follistatin

Analyse Structure of FS1, the heparin-binding domain of follistatin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LR9
Type: protein
Length: 73 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Follistatin
UniProt: P21674

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Follistatin	protein	73	14% helix, 26% strand	P21674

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

1LR9 · STRUCTURE OF Fs1, THE HEPARIN-BINDING DOMAIN OF FOLLISTATIN · the same entry in another collection · chain A against A, TM-score 1.00
P21674 · AlphaFold monomer V2.0 prediction for follistatin (P21674) · a predicted model of the same protein · chain A against A, TM-score 0.91

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P21674
Elsewhere: RCSB PDB 1LR9 · PDBe 1LR9 · UniProt P21674

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