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Joint X-RAY/NEUTRON room temperature structure of perdeuterated pll lectin in complex with perdeuterated L-fucose

Analyse Joint X-RAY/NEUTRON room temperature structure of perdeuterated pll lectin in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BBC
Type: protein
Length: 354 residues
Chains: 1
Method: x-ray diffraction; neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pll lectin
UniProt: A0A329WTS5
Ligands: FUL, FUC
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction; neutron diffraction · 1 distinct chain · 0% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pll lectin	protein	354	0% helix, 48% strand	A0A329WTS5

Ligands and binding sites

FUL · beta-L-fucopyranose · sugar · 3 copies · chains A
FUC · alpha-L-fucopyranose · sugar · 3 copies · 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	848	0.79	0.82	44	empty
2	55	0.32	0.77	13	empty

Compared structures

7BBC · Joint X-ray/neutron room temperature structure of perdeuterated PLL lectin in complex… · 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 A0A329WTS5
Elsewhere: RCSB PDB 7BBC · PDBe 7BBC · UniProt A0A329WTS5

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