Research workbench

Gqqa- a novel type of quorum quenching acylases

Analyse Gqqa- a novel type of quorum quenching acylases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ALZ
Type: protein
Length: 388 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prephenate dehydratase
EC: 4.2.1.51
UniProt: A0A0M0ELU2
Ligands: PHE
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Prephenate dehydratase (EC 4.2.1.51)	protein	194	25% helix, 42% strand	A0A0M0ELU2

Ligands and binding sites

PHE · Phenylalanine · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.77	0.97	29	empty
2	53	0.71	0.98	21	PHE
3	83	0.51	0.84	22	empty
4	70	0.49	0.85	22	empty
5	154	0.46	0.76	22	empty

Interfaces

1 interface between chains.

A–B · 2051 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

7ALZ · GqqA- a novel type of quorum quenching acylases · 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 A0A0M0ELU2
Elsewhere: RCSB PDB 7ALZ · PDBe 7ALZ · UniProt A0A0M0ELU2

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