MolNFT v1 · #117265 · protein

Anti-tau AT8 Fab with triply phosphorylated tau peptide

5E2W · AT8 light chain: “Anti-tau AT8 Fab with triply phosphorylated tau peptide”. X-ray diffraction, 3 pockets (best druggability 0.57). MolNFT v1 #117265 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5E2W
Type: protein
Length: 432 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: 3 · best druggability 0.57

Structure

x-ray diffraction · 3 distinct chains · 6% 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	7% helix, 53% strand	—
P	Tau-phosphopeptide	protein	8	0% helix, 13% strand	—

Pockets

3 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	393	0.57	0.75	46	empty
2	57	0.29	0.75	16	empty
3	57	0.29	0.74	16	empty

Interfaces

3 interfaces between chains.

L–H · 1663 Å² buried · 17 hydrogen bonds · protein-protein
H–P · 382 Å² buried · 7 hydrogen bonds · protein-protein
L–P · 263 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 3 modified (disulfide, phosphorylation).

Compared structures

5E2W · Anti-TAU AT8 FAB with triply 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 5E2W · PDBe 5E2W

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