Research workbench

Crystal structure of ESPRDELTA10, C-terminal 10 amino acids deletion mutant of espr transcription factor from mycobacterium tuberculosis

Analyse Crystal structure of ESPRDELTA10, C-terminal 10 amino acids deletion mutant of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QWG
Type: protein
Length: 183 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esx-1 secretion-associated regulator espr
UniProt: P96228
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esx-1 secretion-associated regulator espr	protein	93	66% helix, 0% strand	P96228
B	Esx-1 secretion-associated regulator espr	protein	90	64% helix, 0% strand	P96228

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	122	0.41	0.76	24	empty
2	85	0.37	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 616 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3QWG · Crystal structure of EspRdelta10, C-terminal 10 amino acids deletion mutant of EspR… · the same entry in another collection · chain A against A, TM-score 1.00

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 P96228
Elsewhere: RCSB PDB 3QWG · PDBe 3QWG · UniProt P96228

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.