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Beta-galactosidase (E. COLI) in the presence of potassium chloride.

Analyse Beta-galactosidase (E. COLI) in the presence of potassium chloride. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TTG
Type: protein
Length: 4,060 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-galactosidase
EC: 3.2.1.23
UniProt: Q8VNN2
Ligands: K, MG, CL
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Beta-galactosidase (EC 3.2.1.23)	protein	1015	14% helix, 41% strand	Q8VNN2

Ligands and binding sites

K · Potassium ion · metal · 16 copies · chains A, B, C, D
MG · Magnesium ion · metal · 14 copies · chains A, B, C, D
CL · Chloride ion · ion · chains A
DMS · Dimethyl sulfoxide · additive · 132 copies · chains A, D, B, C

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1010	0.82	0.83	117	empty
2	798	0.80	0.83	118	DMS
3	709	0.78	0.83	77	empty
4	482	0.77	0.86	90	DMS
5	423	0.72	0.83	42	DMS

Interfaces

6 interfaces between chains.

B–C · 2500 Å² buried · 36 hydrogen bonds · protein-protein
A–D · 2402 Å² buried · 33 hydrogen bonds · protein-protein
C–D · 2040 Å² buried · 31 hydrogen bonds · protein-protein
A–B · 2037 Å² buried · 37 hydrogen bonds · protein-protein
A–C · 144 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (oxidation).

Compared structures

4TTG · Beta-galactosidase (E. coli) in the presence of potassium chloride. · the same entry in another collection · chain D against D, TM-score 1.00
Q8VNN2 · AlphaFold monomer V2.0 prediction for beta-galactosidase (Q8VNN2) · a predicted model of the same protein · chain D 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 Q8VNN2
Elsewhere: RCSB PDB 4TTG · PDBe 4TTG · UniProt Q8VNN2

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