MolNFT v1 · #13304 · protein

Alpha-catenin fragment, residues 385-651

1L7C · Alpha E-catenin: “Alpha-catenin fragment, residues 385-651”. X-ray diffraction, 6 pockets (best druggability 0.78). MolNFT v1 #13304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1L7C
Type: protein
Length: 702 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha E-catenin
UniProt: P35221
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha E-catenin	protein	240	86% helix, 0% strand	P35221
B	Alpha E-catenin	protein	229	85% helix, 0% strand	P35221
C	Alpha E-catenin	protein	233	80% helix, 0% strand	P35221

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1037	0.78	0.80	103	empty
2	342	0.66	0.80	33	empty
3	523	0.66	0.77	63	empty
4	262	0.55	0.77	46	empty
5	176	0.45	0.75	23	empty

Interfaces

3 interfaces between chains.

B–C · 1249 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1013 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 509 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

1L7C · alpha-catenin fragment, residues 385-651 · the same entry in another collection · chain A against A, TM-score 1.00
P35221 · AlphaFold monomer V2.0 prediction for catenin alpha-1 (P35221) · a predicted model of the same protein · chain C against A, TM-score 0.57

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 P35221
Elsewhere: RCSB PDB 1L7C · PDBe 1L7C · UniProt P35221

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.