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Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH 6.5

Analyse Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MP3
Type: protein
Length: 894 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Igh protein; ENSMUSG00000076577 protein; Microtubule-associated protein
UniProt: Q99LC4, Q52L64, A0A024R9Y0
Pockets: 11 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H, A	Igh protein	protein	220	7% helix, 53% strand	Q99LC4
L, B	ENSMUSG00000076577 protein	protein	218	6% helix, 55% strand	Q52L64
C, D	Microtubule-associated protein	protein	9	0% helix, 0% strand	A0A024R9Y0

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	612	0.70	0.78	61	empty
2	603	0.62	0.74	65	empty
3	307	0.56	0.76	41	empty
4	327	0.54	0.75	39	empty
5	215	0.51	0.76	31	empty

Interfaces

11 interfaces between chains.

A–B · 1769 Å² buried · 16 hydrogen bonds · protein-protein
H–L · 1767 Å² buried · 15 hydrogen bonds · protein-protein
H–D · 317 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 301 Å² buried · 4 hydrogen bonds · protein-protein
L–A · 264 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 2 modified (disulfide, cyclization).

Compared structures

5MP3 · Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH 6.5 · the same entry in another collection · chain B against B, 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
Every structure of UniProt Q99LC4
Every structure of UniProt Q52L64
Every structure of UniProt A0A024R9Y0
Elsewhere: RCSB PDB 5MP3 · PDBe 5MP3 · UniProt Q99LC4 · UniProt Q52L64 · UniProt A0A024R9Y0

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