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X-ray structure of the N-terminal domain of human doublecortin

Analyse X-ray structure of the N-terminal domain of human doublecortin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IO9
Type: protein
Length: 193 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuronal migration protein doublecortin
UniProt: O43602
Pockets: 1 · best druggability 0.25

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neuronal migration protein doublecortin	protein	98	15% helix, 23% strand	O43602
B	Neuronal migration protein doublecortin	protein	95	19% helix, 24% strand	O43602

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.25	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 287 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5IO9 · X-ray structure of the N-terminal domain of human doublecortin · the same entry in another collection · chain A against A, TM-score 1.00
O43602 · AlphaFold monomer V2.0 prediction for neuronal migration protein doublecortin (O43602) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O43602
Elsewhere: RCSB PDB 5IO9 · PDBe 5IO9 · UniProt O43602

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