Research workbench

Crystal structure of CB2 Fab

Analyse Crystal structure of CB2 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HFF
Type: protein
Length: 850 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CB2 Fab, light chain; CB2 Fab, heavy chain
Pockets: 11 · best druggability 0.68

Structure

x-ray diffraction · 4 distinct chains · 7% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CB2 Fab, light chain	protein	213	6% helix, 52% strand	—
B	CB2 Fab, heavy chain	protein	214	8% helix, 56% strand	—
L	CB2 Fab, light chain	protein	211	6% helix, 52% strand	—
H	CB2 Fab, heavy chain	protein	212	7% helix, 55% strand	—

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	653	0.68	0.77	68	empty
2	77	0.59	0.89	23	empty
3	406	0.57	0.74	50	empty
4	70	0.54	0.87	23	empty
5	306	0.51	0.73	43	empty

Interfaces

3 interfaces between chains.

L–H · 1711 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1705 Å² buried · 15 hydrogen bonds · protein-protein
B–H · 698 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

2HFF · Crystal structure of CB2 Fab · the same entry in another collection · chain A against A, 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 2HFF · PDBe 2HFF

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