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Crystal structure of E.COLI DNA gyrase B in complex with 2-oxo-1,2- dihydroquinoline derivative

Analyse Crystal structure of E.COLI DNA gyrase B in complex with 2-oxo-1,2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KZZ
Type: protein
Length: 196 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA gyrase subunit B
EC: 5.6.2.2
UniProt: A0A4V5JMQ9
Ligands: E0R
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA gyrase subunit B (EC 5.6.2.2)	protein	196	33% helix, 29% strand	A0A4V5JMQ9

Ligands and binding sites

E0R · 4-[[8-(methylamino)-2-oxidanylidene-1~{H}-quinolin-3-yl]carbonylamino]benzoic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.51	0.81	20	E0R
2	51	0.34	0.78	15	empty

Compared structures

6KZZ · Crystal structure of E.coli DNA gyrase B in complex with 2-oxo-1,2-dihydroquinoline… · 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 A0A4V5JMQ9
Elsewhere: RCSB PDB 6KZZ · PDBe 6KZZ · UniProt A0A4V5JMQ9

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