Research workbench

Deactivation of human IGG1 Fc by endoglycosidase treatment

Analyse Deactivation of human IGG1 Fc by endoglycosidase treatment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ACP
Type: protein
Length: 406 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ig gamma-1 chain C region
UniProt: P01857
Ligands: NAG
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ig gamma-1 chain C region	protein	198	12% helix, 48% strand	P01857
B	Ig gamma-1 chain C region	protein	208	11% helix, 49% strand	P01857

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	157	0.40	0.73	32	empty
2	55	0.29	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1187 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

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

Compared structures

4ACP · Deactivation of human IgG1 Fc by endoglycosidase treatment · 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 P01857
Elsewhere: RCSB PDB 4ACP · PDBe 4ACP · UniProt P01857

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