MolNFT v1 · #107723 · protein

Crystal structure of quinine-dependent Fab 314.3 with quinine

4UIN: “Crystal structure of quinine-dependent Fab 314.3 with quinine”. X-ray diffraction, 1 ligand (QI9), 9 pockets (best druggability 0.45). MolNFT v1 #107723 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4UIN
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab 314.3
Ligands: QI9
Pockets: 9 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Fab 314.3	protein	221	5% helix, 52% strand	—
L	Fab 314.3	protein	214	5% helix, 52% 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

9 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	139	0.45	0.76	25	empty
2	72	0.43	0.81	18	QI9
3	135	0.40	0.74	27	empty
4	100	0.38	0.75	24	empty
5	51	0.37	0.80	13	empty

Interfaces

1 interface between chains.

H–L · 1786 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

4UIN · crystal structure of quinine-dependent Fab 314.3 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 4UIN · PDBe 4UIN

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