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Enzyme deglycosylated human IGG1 Fc fragment

Analyse Enzyme deglycosylated human IGG1 Fc fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DNK
Type: protein
Length: 419 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ighm protein
UniProt: Q6PI81
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ighm protein	protein	209	11% helix, 48% strand	Q6PI81
B	Ighm protein	protein	210	10% helix, 48% strand	Q6PI81

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	67	0.29	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 1204 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3DNK · Enzyme deglycosylated Human IgG1 Fc fragment · 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 Q6PI81
Elsewhere: RCSB PDB 3DNK · PDBe 3DNK · UniProt Q6PI81

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