Research workbench

Crystal structure of bar domain of endophilin-III

Analyse Crystal structure of bar domain of endophilin-III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z0V
Type: protein
Length: 444 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SH3-containing GRB2-like protein 3
UniProt: Q99963
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SH3-containing GRB2-like protein 3	protein	223	81% helix, 0% strand	Q99963
B	SH3-containing GRB2-like protein 3	protein	221	79% helix, 1% strand	Q99963

Pockets

4 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	118	0.79	0.98	22	empty
2	117	0.46	0.78	25	empty
3	75	0.39	0.78	19	empty
4	57	0.29	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 3146 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

2Z0V · Crystal structure of BAR domain of Endophilin-III · the same entry in another collection · chain A against A, TM-score 1.00
Q99963 · AlphaFold monomer V2.0 prediction for endophilin-A3 (Q99963) · a predicted model of the same protein · chain A 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 Q99963
Elsewhere: RCSB PDB 2Z0V · PDBe 2Z0V · UniProt Q99963

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