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Crystal structure of neurofascin adhesion complex in space group P3221

Analyse Crystal structure of neurofascin adhesion complex in space group P3221 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P40
Type: protein
Length: 390 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurofascin
UniProt: O94856
Ligands: NAG
Pockets: 3 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neurofascin	protein	390	2% helix, 42% strand	O94856

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.32	0.76	13	empty
2	55	0.30	0.76	10	NAG
3	60	0.29	0.74	15	empty

Modifications

Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

3P40 · Crystal structure of neurofascin adhesion complex in space group p3221 · the same entry in another collection · chain A against A, TM-score 1.00
O94856 · AlphaFold monomer V2.0 prediction for neurofascin (O94856) · 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 O94856
Elsewhere: RCSB PDB 3P40 · PDBe 3P40 · UniProt O94856

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