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Domain swapping in the cytoplasmic domain of the escherichia COLI rhomboid protease

Analyse Domain swapping in the cytoplasmic domain of the escherichia COLI rhomboid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HDD
Type: protein
Length: 66 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rhomboid protease glpg
EC: 3.4.21.105
UniProt: P09391
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rhomboid protease glpg (EC 3.4.21.105)	protein	66	50% helix, 0% strand	P09391

Ligands and binding sites

ACT · Acetate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	114	0.43	0.77	18	empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

4HDD · Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease · the same entry in another collection · chain A against A, TM-score 1.00
P09391 · AlphaFold monomer V2.0 prediction for rhomboid protease glpg (P09391) · a predicted model of the same protein · chain A against A, TM-score 0.50

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 P09391
Elsewhere: RCSB PDB 4HDD · PDBe 4HDD · UniProt P09391

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