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E. COLI DNA gyrase B 24 kda ATPase domain in complex with 1-ethyl-3- [5-pyridin-4-yl-8-(pyridin-3-ylamino)-isoquinolin-3-yl]-urea

Analyse E. COLI DNA gyrase B 24 kda ATPase domain in complex with 1-ethyl-3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MMP
Type: protein
Length: 191 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA gyrase subunit B
EC: 5.99.1.3
UniProt: P0AES7
Ligands: G3Z
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA gyrase subunit B (EC 5.99.1.3)	protein	191	32% helix, 29% strand	P0AES7

Ligands and binding sites

G3Z · 1-ethyl-3-[5-pyridin-4-yl-8-(pyridin-3-ylamino) isoquinolin-3-yl]urea · ligand · 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	86	0.47	0.81	18	G3Z

Compared structures

5MMP · E. coli DNA Gyrase B 24 kDa ATPase domain in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P0AES7 · AlphaFold monomer V2.0 prediction for DNA gyrase subunit B (P0AES7) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P0AES7
Elsewhere: RCSB PDB 5MMP · PDBe 5MMP · UniProt P0AES7

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