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Crystal structures of a formin homology-2 domain reveal a tethered- dimer architecture

Analyse Crystal structures of a formin homology-2 domain reveal a tethered- dimer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UX4
Type: protein
Length: 820 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BNI1 protein
UniProt: P41832
Pockets: 11 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	BNI1 protein	protein	410	57% helix, 1% strand	P41832

Pockets

11 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	359	0.65	0.80	23	empty
2	137	0.45	0.76	16	empty
3	163	0.45	0.75	26	empty
4	114	0.43	0.77	16	empty
5	125	0.41	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 630 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1UX4 · Crystal structures of a Formin Homology-2 domain reveal a tethered-dimer architecture · the same entry in another collection · chain A against A, TM-score 1.00
P41832 · AlphaFold monomer V2.0 prediction for protein BNI1 (P41832) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P41832
Elsewhere: RCSB PDB 1UX4 · PDBe 1UX4 · UniProt P41832

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