Research workbench

Crystal structure of HCR/D-sa-GBL1/C

Analyse Crystal structure of HCR/D-sa-GBL1/C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FVV
Type: protein
Length: 827 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neurotoxin
UniProt: Q9LBR1
Ligands: SIA, SO4
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neurotoxin	protein	412	8% helix, 49% strand	Q9LBR1
B	Neurotoxin	protein	415	8% helix, 48% strand	Q9LBR1

Ligands and binding sites

SIA · N-acetyl-alpha-neuraminic acid · sugar · chains B
SO4 · Sulfate ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	894	0.76	0.79	88	GOL
2	300	0.60	0.79	39	empty
3	113	0.48	0.80	25	empty
4	100	0.47	0.80	19	empty
5	67	0.39	0.79	22	empty

Interfaces

1 interface between chains.

A–B · 540 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4FVV · Crystal structure of HCR/D-Sa-GBL1/C · the same entry in another collection · chain B against B, 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 Q9LBR1
Elsewhere: RCSB PDB 4FVV · PDBe 4FVV · UniProt Q9LBR1

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