MolNFT v1 · #88423 · protein

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

4CU9: “Unravelling the multiple functions of the architecturally intricate streptococcus pneumoniae…”. X-ray diffraction, 1 ligand (CA), 2 pockets (best druggability 0.73). MolNFT v1 #88423 on GenesisL1: 3D structure, binding sites and…

PDB: 4CU9
Type: protein
Length: 358 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-galactosidase
UniProt: Q8DQP4
Ligands: CA
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-galactosidase	protein	173	9% helix, 40% strand	Q8DQP4
B	Beta-galactosidase	protein	185	8% helix, 37% strand	Q8DQP4

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

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	807	0.73	0.78	74	EDO
2	53	0.25	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 444 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4CU9 · 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 Q8DQP4
Elsewhere: RCSB PDB 4CU9 · PDBe 4CU9 · UniProt Q8DQP4

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