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Crystal structure of E. COLI gyrase B co-complexed with prop-2-yn-1-yl {[5-(4-piperidin-1-yl-2-pyridin-3-yl-1,3-thiazol-5-yl)-1H-pyrazol-3- YL]METHYL}CARBAMATE inhibitor

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

PDB: 3G7E
Type: protein
Length: 203 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: C3SLN3
Ligands: B46
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA gyrase subunit B (EC 5.99.1.3)	protein	203	27% helix, 29% strand	C3SLN3

Ligands and binding sites

B46 · prop-2-yn-1-yl {[5-(4-piperidin-1-yl-2-pyridin-3-yl-1,3-thiazol-5-yl)-1H-pyrazol-3-yl]methyl}carbamate · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	230	0.75	0.89	40	B46

Compared structures

3G7E · Crystal structure of E. coli Gyrase B co-complexed with PROP-2-YN-1-YL… · 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 C3SLN3
Elsewhere: RCSB PDB 3G7E · PDBe 3G7E · UniProt C3SLN3

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