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NMR structure of the Y174 autoinhibited dbl homology domain

Analyse NMR structure of the Y174 autoinhibited dbl homology domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F5X
Type: protein
Length: 208 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho-gef vav
UniProt: P27870
Pockets: 1 · best druggability 0.61

Structure

solution nmr · 1 distinct chain · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rho-gef vav	protein	208	69% helix, 0% strand	P27870

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	211	0.61	0.81	20	empty

Compared structures

1F5X · NMR structure of the Y174 autoinhibited dbl homology domain · the same entry in another collection · chain A against A, TM-score 1.00
P27870 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P27870) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P27870
Elsewhere: RCSB PDB 1F5X · PDBe 1F5X · UniProt P27870

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