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Solution NMR studies of the dimeric regulatory subunit ilvn of the E.COLI acetohydroxyacid synthase I (ahas I)

Analyse Solution NMR studies of the dimeric regulatory subunit ilvn of the E.COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LVW
Type: protein
Length: 196 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetolactate synthase isozyme 1 small subunit
EC: 2.2.1.6
UniProt: P0ADF8
Pockets: 2 · best druggability 0.47

Structure

solution nmr · 1 distinct chain · 30% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6)	protein	98	30% helix, 33% strand	P0ADF8

Pockets

2 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	179	0.47	0.76	26	empty
2	163	0.45	0.75	26	empty

Interfaces

1 interface between chains.

A–B · 1035 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2LVW · Solution NMR studies of the dimeric regulatory subunit IlvN of the E.coli… · the same entry in another collection · chain A against A, TM-score 1.00
P0ADF8 · AlphaFold monomer V2.0 prediction for acetolactate synthase isozyme 1 small subunit… · a predicted model of the same protein · chain A against A, TM-score 0.80

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 P0ADF8
Elsewhere: RCSB PDB 2LVW · PDBe 2LVW · UniProt P0ADF8

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