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Crystal structure of the N-bar domain of human bridging integrator 2.

Analyse Crystal structure of the N-bar domain of human bridging integrator 2. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AVM
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bridging integrator 2
UniProt: Q9UBW5
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 88% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bridging integrator 2	protein	230	88% helix, 0% strand	Q9UBW5

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	123	0.45	0.77	18	empty
2	61	0.35	0.77	12	empty
3	59	0.28	0.74	15	empty

Compared structures

4AVM · Crystal structure of the N-BAR domain of human bridging integrator 2. · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBW5 · AlphaFold monomer V2.0 prediction for bridging integrator 2 (Q9UBW5) · 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 Q9UBW5
Elsewhere: RCSB PDB 4AVM · PDBe 4AVM · UniProt Q9UBW5

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