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Antigen binding fragment of an anti IFNAR1 antibody

Analyse Antigen binding fragment of an anti IFNAR1 antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QXG
Type: protein
Length: 432 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab, heavy chain, IGG1; Fab, light chain, IGG1
Ligands: K, PO4
Pockets: 5 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Fab, heavy chain, IGG1	protein	218	11% helix, 54% strand	—
L	Fab, light chain, IGG1	protein	214	7% helix, 54% strand	—

Ligands and binding sites

K · Potassium ion · metal · chains H
PO4 · Phosphate ion · ion · chains H, L
GOL · Glycerol · additive · chains H, L

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	521	0.61	0.75	52	empty
2	54	0.46	0.85	21	GOL
3	119	0.41	0.76	24	empty
4	94	0.34	0.74	18	empty
5	71	0.31	0.74	16	empty

Interfaces

1 interface between chains.

H–L · 1892 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4QXG · Antigen binding fragment of an anti IFNAR1 antibody · the same entry in another collection · chain H against H, 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
Elsewhere: RCSB PDB 4QXG · PDBe 4QXG

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