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X11 ptb domain-10MER peptide complex

Analyse X11 ptb domain-10MER peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AQC
Type: protein
Length: 272 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: X11; Peptide
UniProt: Q02410
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	X11	protein	130	33% helix, 41% strand	Q02410
C, D	Peptide	protein	10	40% helix, 20% strand	—
B	X11	protein	122	34% helix, 39% strand	Q02410

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.36	0.74	16	empty
2	62	0.32	0.76	12	empty

Interfaces

3 interfaces between chains.

A–C · 786 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 656 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 609 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

1AQC · X11 ptb domain-10MER peptide complex · the same entry in another collection · chain A against A, TM-score 1.00
Q02410 · AlphaFold monomer V2.0 prediction for amyloid-beta A4 precursor protein-binding family a… · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q02410
Elsewhere: RCSB PDB 1AQC · PDBe 1AQC · UniProt Q02410

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