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Crystal structure of bacteriocin as-48. N-decyl-beta-D-maltoside bound.

Analyse Crystal structure of bacteriocin as-48. N-decyl-beta-D-maltoside bound. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O84
Type: protein
Length: 140 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide antibiotic as-48
UniProt: Q47765
Ligands: D10, GLC, SO4
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Peptide antibiotic as-48	protein	70	79% helix, 0% strand	Q47765

Ligands and binding sites

D10 · Decane · ligand · chains A, B
GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A, B
GOL · Glycerol · additive · chains A, B

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	187	0.55	0.79	20	GOL, SO4

Interfaces

1 interface between chains.

A–B · 475 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1O84 · Crystal Structure of Bacteriocin AS-48. N-decyl-beta-D-maltoside Bound. · 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 Q47765
Elsewhere: RCSB PDB 1O84 · PDBe 1O84 · UniProt Q47765

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