MolNFT v1 · #107721 · protein

Crystal structure of quinine-dependent Fab 314.1 with quinine

4UIL: “Crystal structure of quinine-dependent Fab 314.1 with quinine”. X-ray diffraction, 1 ligand (QI9), 7 pockets (best druggability 0.42). MolNFT v1 #107721 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4UIL
Type: protein
Length: 431 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab 314.1
Ligands: QI9
Pockets: 7 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Fab 314.1	protein	218	5% helix, 46% strand	—
L	Fab 314.1	protein	213	5% helix, 43% strand	—

Ligands and binding sites

QI9 · Quinine · ligand · chains H, L

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

Pockets

7 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	75	0.42	0.80	17	QI9
2	170	0.40	0.73	36	empty
3	82	0.39	0.78	21	empty
4	106	0.38	0.75	24	empty
5	64	0.30	0.74	17	empty

Interfaces

1 interface between chains.

H–L · 1877 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4UIL · crystal structure of quinine-dependent Fab 314.1 with quinine · 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 4UIL · PDBe 4UIL

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.