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Foldon domain wild type C-conjugate

Analyse Foldon domain wild type C-conjugate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NCW
Type: protein
Length: 73 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fibritin
UniProt: D9IEJ2
Ligands: 2KN
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fibritin	protein	25	12% helix, 32% strand	D9IEJ2
B, C	Fibritin	protein	24	13% helix, 38% strand	D9IEJ2

Ligands and binding sites

2KN · N,N',N''-triethylbenzene-1,3,5-tricarboxamide · ligand · chains A, B, C

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

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	51	0.27	0.74	13	empty

Interfaces

3 interfaces between chains.

A–C · 438 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 400 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 399 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4NCW · foldon domain wild type C-conjugate · the same entry in another collection · chain A against A, TM-score 1.00

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 D9IEJ2
Elsewhere: RCSB PDB 4NCW · PDBe 4NCW · UniProt D9IEJ2

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