Research workbench

Crystal structure of the hemolytic lectin from the mushroom laetiporus sulphureus complexed with N-acetyllactosamine in the gamma motif

Analyse Crystal structure of the hemolytic lectin from the mushroom laetiporus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W3F
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemolytic lectin from laetiporus sulphureus
UniProt: Q7Z8V1
Ligands: NDG, GAL
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemolytic lectin from laetiporus sulphureus	protein	312	7% helix, 53% strand	Q7Z8V1

Ligands and binding sites

NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
GAL · beta-D-galactopyranose · sugar · chains A
GOL · Glycerol · additive · 5 copies · 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	161	0.49	0.77	24	empty

Compared structures

1W3F · Crystal structure of the hemolytic lectin from the mushroom Laetiporus sulphureus… · 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 Q7Z8V1
Elsewhere: RCSB PDB 1W3F · PDBe 1W3F · UniProt Q7Z8V1

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