Research workbench

Crystal structure of a putative lipoprotein (ACTODO_00931) from actinomyces odontolyticus atcc 17982 at 2.35 a resolution

Analyse Crystal structure of a putative lipoprotein (ACTODO_00931) from actinomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UP9
Type: protein
Length: 239 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
UniProt: A7BBB2
Ligands: MSE
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein	protein	239	38% helix, 25% strand	A7BBB2

Ligands and binding sites

MSE · Selenomethionine · ligand · chains A
PG4 · Tetraethylene glycol · additive · 4 copies · chains A
PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · 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	78	0.40	0.79	21	empty

Compared structures

3UP9 · Crystal structure of a putative lipoprotein (ACTODO_00931) from Actinomyces odontolyticus… · 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 A7BBB2
Elsewhere: RCSB PDB 3UP9 · PDBe 3UP9 · UniProt A7BBB2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.