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Fab antigen complex

Analyse Fab antigen complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WIO
Type: protein
Length: 545 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab heavy chain; Fab light chain; Interleukin-17A
UniProt: Q16552
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fab heavy chain	protein	230	8% helix, 53% strand	—
B	Fab light chain	protein	213	7% helix, 52% strand	—
C	Interleukin-17A	protein	102	4% helix, 40% strand	Q16552

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	300	0.59	0.78	38	empty
2	426	0.58	0.75	54	empty
3	78	0.34	0.75	15	empty

Interfaces

3 interfaces between chains.

A–B · 1690 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 491 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 273 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

6WIO · Fab antigen complex · the same entry in another collection · chain A against A, TM-score 1.00
Q16552 · AlphaFold monomer V2.0 prediction for interleukin-17A (Q16552) · a predicted model of the same protein · chain C against A, TM-score 0.78

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 Q16552
Elsewhere: RCSB PDB 6WIO · PDBe 6WIO · UniProt Q16552

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