Research workbench

Crystal structure of the propionibacterium acnes surface sialidase in complex with NEU5AC2EN

Analyse Crystal structure of the propionibacterium acnes surface sialidase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LBV
Type: protein
Length: 380 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exo-alpha-sialidase
UniProt: A0A2B7IY20
Ligands: DAN, PO4
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-alpha-sialidase	protein	380	2% helix, 43% strand	A0A2B7IY20

Ligands and binding sites

DAN · 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid · ligand · chains A
PO4 · Phosphate ion · ion · 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	160	0.83	0.98	24	empty
2	110	0.47	0.79	19	DAN

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7LBV · Crystal structure of the Propionibacterium acnes surface sialidase in complex with… · 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 A0A2B7IY20
Elsewhere: RCSB PDB 7LBV · PDBe 7LBV · UniProt A0A2B7IY20

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