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Structure of pqs response protein pqse in complex with N-(4-(3- NEOPENTYLUREIDO)PHENYL)-1H-indazole-7-carboxamide

Analyse Structure of pqs response protein pqse in complex with N-(4-(3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TZA
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quinolone signal response protein
UniProt: A0A0H2Z6F6
Ligands: KYX, FE
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Quinolone signal response protein	protein	296	37% helix, 23% strand	A0A0H2Z6F6

Ligands and binding sites

KYX · N-{4-[(2,2-dimethylpropyl)carbamamido]phenyl}-1H-indazole-7-carboxamide · ligand · chains A
FE · Fe (III) ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	267	0.64	0.81	31	KYX

Compared structures

7TZA · Structure of PQS Response Protein PqsE in complex with… · 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 A0A0H2Z6F6
Elsewhere: RCSB PDB 7TZA · PDBe 7TZA · UniProt A0A0H2Z6F6

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