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Unravelling the multiple functions of the architecturally intricate streptococcus pneumoniae beta-galactosidase, bgaa

Analyse Unravelling the multiple functions of the architecturally intricate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CU8
Type: protein
Length: 848 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase 2
UniProt: I6L8R4
Ligands: DGJ, SO4
Pockets: 12 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase 2	protein	848	16% helix, 38% strand	I6L8R4

Ligands and binding sites

DGJ · (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 50 copies · chains A

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

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	701	0.78	0.83	67	EDO, SO4
2	83	0.76	0.98	22	EDO
3	289	0.67	0.82	26	EDO
4	396	0.60	0.76	41	EDO
5	190	0.57	0.80	30	EDO

Compared structures

4CU8 · Unravelling the multiple functions of the architecturally intricate Streptococcus… · 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 I6L8R4
Elsewhere: RCSB PDB 4CU8 · PDBe 4CU8 · UniProt I6L8R4

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