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Crystal structure of the antiflavivirus FAB4G2

Analyse Crystal structure of the antiflavivirus FAB4G2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UYW
Type: protein
Length: 859 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab antibody heavy chain; Fab antibody light chain
Pockets: 8 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H, M	Fab antibody heavy chain	protein	218	7% helix, 52% strand	—
L	Fab antibody light chain	protein	212	7% helix, 52% strand	—
N	Fab antibody light chain	protein	211	7% helix, 53% strand	—

Pockets

8 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	869	0.79	0.82	99	empty
2	558	0.62	0.74	61	empty
3	219	0.49	0.75	28	empty
4	103	0.48	0.81	26	empty
5	119	0.39	0.75	18	empty

Interfaces

5 interfaces between chains.

M–N · 1895 Å² buried · 14 hydrogen bonds · protein-protein
H–L · 1868 Å² buried · 12 hydrogen bonds · protein-protein
H–M · 344 Å² buried · 3 hydrogen bonds · protein-protein
L–M · 247 Å² buried · 2 hydrogen bonds · protein-protein
H–N · 74 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1UYW · Crystal Structure of the antiflavivirus Fab4g2 · 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 1UYW · PDBe 1UYW

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