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Structure of the human line-1 ORF1P central domain

Analyse Structure of the human line-1 ORF1P central domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W7A
Type
protein
Length
199 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Line-1 ORF1P
UniProt
Q15605
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALine-1 ORF1Pprotein10035% helix, 28% strandQ15605
BLine-1 ORF1Pprotein9935% helix, 29% strandQ15605

Ligands and binding sites

  • MLI · Malonate ion · additive · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11790.570.8121empty
2560.280.7417empty

Interfaces

1 interface between chains.

  • A–B · 615 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 2W7A · Structure of the human LINE-1 ORF1p central domain · the same entry in another collection · chain A against A, TM-score 1.00

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