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Cyrstal structure of anti-tau antibody cbtau-22.1 Fab

Analyse Cyrstal structure of anti-tau antibody cbtau-22.1 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5V7U
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cbtau-22.1 Fab light chain; Cbtau-22.1 Fab heavy chain
Ligands: SO4
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	Cbtau-22.1 Fab light chain	protein	219	6% helix, 49% strand	—
H	Cbtau-22.1 Fab heavy chain	protein	216	10% helix, 51% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains L, H

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	295	0.59	0.78	43	empty
2	148	0.40	0.73	26	empty
3	74	0.35	0.77	21	SO4
4	80	0.34	0.75	21	empty
5	52	0.28	0.75	15	empty

Interfaces

1 interface between chains.

L–H · 1788 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

5V7U · Cyrstal structure of anti-Tau antibody CBTAU-22.1 Fab · the same entry in another collection · chain L against L, 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 5V7U · PDBe 5V7U

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