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Structure of streptococcus pneumonia pare in complex with AZ13072886

Analyse Structure of streptococcus pneumonia pare in complex with AZ13072886 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MOT
Type: protein
Length: 193 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Topoisomerase IV subunit B
EC: 5.99.1.-
UniProt: Q8DQB5
Ligands: 2B7
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Topoisomerase IV subunit B (EC 5.99.1.-)	protein	193	33% helix, 30% strand	Q8DQB5

Ligands and binding sites

2B7 · 1-[4-(3-methylbutyl)-5-oxo-6-(pyridin-3-yl)-4,5-dihydro[1,3]thiazolo[5,4-b]pyridin-2-yl]-3-prop-2-en-1-ylurea · 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	120	0.46	0.78	25	2B7

Compared structures

4MOT · Structure of Streptococcus pneumonia pare in complex with AZ13072886 · 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 Q8DQB5
Elsewhere: RCSB PDB 4MOT · PDBe 4MOT · UniProt Q8DQB5

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