MolNFT v1 · #137494 · protein

Beta-glucoside phosphorylase bglx

5VQD: “Beta-glucoside phosphorylase bglx”. X-ray diffraction, 4 pockets (best druggability 0.67). MolNFT v1 #137494 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5VQD
Type: protein
Length: 555 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucoside phosphorylase bglx
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucoside phosphorylase bglx	protein	555	41% helix, 13% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 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	219	0.67	0.85	35	GOL
2	158	0.45	0.76	28	empty
3	129	0.43	0.76	22	empty
4	50	0.24	0.72	12	empty

Compared structures

5VQD · Beta-glucoside phosphorylase BglX · 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
Elsewhere: RCSB PDB 5VQD · PDBe 5VQD

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