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E. COLI (lacz) beta-galactosidase (S796D)

Analyse E. COLI (lacz) beta-galactosidase (S796D) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3T2O
Type
protein
Length
4,044 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-galactosidase
EC
3.2.1.23
UniProt
P00722
Ligands
MG, NA
Pockets
20 · best druggability 0.84

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DBeta-galactosidase (EC 3.2.1.23)protein101114% helix, 41% strandP00722

Ligands and binding sites

  • MG · Magnesium ion · metal · 16 copies · chains A, B, C, D
  • NA · Sodium ion · metal · 16 copies · chains A, B, C, D
  • DMS · Dimethyl sulfoxide · additive · 112 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19420.840.85151DMS
211170.820.83126empty
310970.820.83114empty
47430.780.83105DMS
55340.730.8267DMS

Interfaces

6 interfaces between chains.

  • B–C · 2394 Ų buried · 34 hydrogen bonds · protein-protein
  • A–D · 2383 Ų buried · 34 hydrogen bonds · protein-protein
  • C–D · 2083 Ų buried · 30 hydrogen bonds · protein-protein
  • A–B · 2072 Ų buried · 34 hydrogen bonds · protein-protein
  • A–C · 141 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3T2O · E. coli (lacZ) beta-galactosidase (S796D) · the same entry in another collection · chain D against D, TM-score 1.00
  • P00722 · AlphaFold monomer V2.0 prediction for beta-galactosidase (P00722) · a predicted model of the same protein · chain D against A, TM-score 1.00

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