MolNFT v1 · #52340 · protein

Structure of il-17A in complex with a potent, fully human neutralising antibody

2VXS · Interleukin-17A: “Structure of il-17A in complex with a potent, fully human neutralising antibody”. X-ray diffraction, 1 ligand (SO4), 20 pockets (best druggability 0.72). MolNFT v1 #52340 on GenesisL1: 3D structure, binding sites…

PDB: 2VXS
Type: protein
Length: 2,043 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interleukin-17A; Fab fragment
UniProt: Q16552
Ligands: SO4
Pockets: 20 · best druggability 0.72

Structure

x-ray diffraction · 10 distinct chains · 8% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interleukin-17A	protein	86	8% helix, 49% strand	Q16552
B, C	Interleukin-17A	protein	80	9% helix, 50% strand	Q16552
D	Interleukin-17A	protein	77	9% helix, 47% strand	Q16552
H	Fab fragment	protein	216	6% helix, 53% strand	—
I	Fab fragment	protein	221	8% helix, 52% strand	—
J	Fab fragment	protein	211	7% helix, 53% strand	—
K	Fab fragment	protein	217	8% helix, 49% strand	—
L, N	Fab fragment	protein	213	9% helix, 49% strand	—
M	Fab fragment	protein	215	9% helix, 49% strand	—
O	Fab fragment	protein	214	7% helix, 47% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 12 copies · chains A, B, L, C, D, N, I, H, M, J, O

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	482	0.72	0.81	61	empty
2	411	0.69	0.81	57	empty
3	316	0.66	0.81	36	empty
4	255	0.62	0.81	34	empty
5	154	0.58	0.83	31	empty

Interfaces

22 interfaces between chains.

I–M · 1808 Å² buried · 20 hydrogen bonds · protein-protein
K–O · 1762 Å² buried · 18 hydrogen bonds · protein-protein
H–L · 1744 Å² buried · 18 hydrogen bonds · protein-protein
J–N · 1731 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1307 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 25 disulfide (disulfide).

Compared structures

2VXS · Structure of IL-17A in complex with a potent, fully human neutralising antibody · the same entry in another collection · chain O against O, 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 Q16552
Elsewhere: RCSB PDB 2VXS · PDBe 2VXS · UniProt Q16552

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