MolNFT v1 · #105711 · protein

X-ray structure of the apo form of the amyloid precursor protein-like protein 1 (APLP1) E2 domain

4RD9 · Amyloid-like protein 1: “X-ray structure of the apo form of the amyloid precursor protein-like protein 1 (APLP1) E2 domain”. X-ray diffraction, 5 pockets (best druggability 0.68). MolNFT v1 #105711 on GenesisL1: 3D structure…

PDB: 4RD9
Type: protein
Length: 376 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amyloid-like protein 1
UniProt: P51693
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amyloid-like protein 1	protein	188	91% helix, 0% strand	P51693
B	Amyloid-like protein 1	protein	188	89% helix, 0% strand	P51693

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	794	0.68	0.75	62	empty
2	50	0.62	0.93	18	empty
3	224	0.55	0.78	35	empty
4	60	0.37	0.79	14	empty
5	53	0.34	0.78	11	empty

Interfaces

1 interface between chains.

A–B · 1887 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

4RD9 · X-ray structure of the apo form of the amyloid precursor protein-like protein 1 (APLP1)… · the same entry in another collection · chain A against A, TM-score 1.00
P51693 · AlphaFold monomer V2.0 prediction for amyloid-like protein 1 (P51693) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P51693
Elsewhere: RCSB PDB 4RD9 · PDBe 4RD9 · UniProt P51693

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