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Solution NMR structures of two alternative conformations of E. COLI tryptophan repressor in dynamic equilibrium

Analyse Solution NMR structures of two alternative conformations of E. COLI tryptophan… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TM0
Type: protein
Length: 432 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRP operon repressor
UniProt: P0A882
Pockets: 2 · best druggability 0.47

Structure

solution nmr · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	TRP operon repressor	protein	108	76% helix, 0% strand	P0A882

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	116	0.47	0.79	21	empty
2	125	0.45	0.78	21	empty

Interfaces

2 interfaces between chains.

A–B · 2432 Å² buried · 21 hydrogen bonds · protein-protein
C–D · 2329 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5TM0 · Solution NMR structures of two alternative conformations of E. coli tryptophan repressor… · the same entry in another collection · chain D against D, TM-score 1.00
P0A882 · AlphaFold monomer V2.0 prediction for TRP operon repressor (P0A882) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P0A882
Elsewhere: RCSB PDB 5TM0 · PDBe 5TM0 · UniProt P0A882

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