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Swirm domain of human LSD1

Analyse Swirm domain of human LSD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IT3
Type
protein
Length
170 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysine-specific histone demethylase 1A
UniProt
O60341
Ligands
MG
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLysine-specific histone demethylase 1Aprotein8558% helix, 0% strandO60341

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11530.490.7822empty
21280.400.7516empty

Interfaces

1 interface between chains.

  • A–B · 380 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 5IT3 · Swirm domain of human Lsd1 · the same entry in another collection · chain A against A, TM-score 1.00

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