MolNFT v2 · #220072 · protein

Structure of the complex formed by human interleukin-2 and scFv F10

8SOW · F10 single chain fragment variable: “Structure of the complex formed by human interleukin-2 and scFv F10”. X-ray diffraction at 1.71, 4 pockets (best druggability 0.28). MolNFT v2 #220072 on GenesisL1: 3D structure, binding sites…

PDB: 8SOW
Type: protein
Length: 335 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.71
Source: Homo sapiens
Molecule: F10 single chain fragment variable; Interleukin-2
UniProt: P60568
Pockets: 4 · best druggability 0.28

Structure

x-ray diffraction · resolution 1.71 · 2 distinct chains · 24% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	F10 single chain fragment variable	protein	219	3% helix, 48% strand	—
A	Interleukin-2	protein	116	64% helix, 3% strand	P60568

Pockets

4 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	62	0.28	0.73	20	empty
2	51	0.27	0.74	12	empty
3	66	0.27	0.72	19	empty
4	50	0.25	0.73	21	empty

Interfaces

1 interface between chains.

C–A · 818 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

P60568 · AlphaFold monomer V2.0 prediction for interleukin-2 (P60568) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P60568
Elsewhere: RCSB PDB 8SOW · PDBe 8SOW · UniProt P60568

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