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Anti-tau AT8 Fab with doubly phosphorylated tau peptide

Analyse Anti-tau AT8 Fab with doubly phosphorylated tau peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E2V
Type: protein
Length: 433 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AT8 light chain; AT8 heavy chain; Tau phosphopeptide
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	AT8 light chain	protein	216	6% helix, 50% strand	—
H	AT8 heavy chain	protein	208	9% helix, 53% strand	—
P	Tau phosphopeptide	protein	9	0% helix, 11% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains L, H, P

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

Pockets

2 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	467	0.57	0.74	47	empty
2	51	0.27	0.74	16	empty

Interfaces

3 interfaces between chains.

L–H · 1678 Å² buried · 14 hydrogen bonds · protein-protein
H–P · 334 Å² buried · 6 hydrogen bonds · protein-protein
L–P · 275 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 modified (disulfide, phosphorylation).

Compared structures

5E2V · Anti-TAU AT8 FAB with doubly phosphorylated TAU peptide · 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 5E2V · PDBe 5E2V

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