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NMR solution structure of the frb domain of mtor

Analyse NMR solution structure of the frb domain of mtor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GAQ
Type: protein
Length: 100 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FKBP12-rapamycin complex-associated protein
UniProt: P42345
Pockets: 1 · best druggability 0.42

Structure

solution nmr · 1 distinct chain · 62% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FKBP12-rapamycin complex-associated protein	protein	100	62% helix, 0% strand	P42345

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.42	0.81	14	empty

Compared structures

2GAQ · NMR SOLUTION STRUCTURE OF THE FRB DOMAIN OF mTOR · the same entry in another collection · chain A against A, TM-score 1.00
P42345 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase mtor (P42345) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 P42345
Elsewhere: RCSB PDB 2GAQ · PDBe 2GAQ · UniProt P42345

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