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Lasr-TP4 complex

Analyse Lasr-TP4 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3JPU
Type
protein
Length
808 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcriptional activator protein lasr
UniProt
P25084
Ligands
TY4
Pockets
10 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, ETranscriptional activator protein lasrprotein16152% helix, 17% strandP25084
CTranscriptional activator protein lasrprotein16350% helix, 17% strandP25084
DTranscriptional activator protein lasrprotein16251% helix, 17% strandP25084

Ligands and binding sites

  • TY4 · 4-bromo-2-({[(2-chlorophenyl)carbonyl]amino}methyl)-6-methylphenyl 2,4-dichlorobenzoate · ligand · 5 copies · chains A, B, C, D, E

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12090.830.9630TY4
21900.810.9529TY4
32180.810.9430TY4
42420.810.9331TY4
52070.800.9433TY4

Interfaces

6 interfaces between chains.

  • B–C · 949 Ų buried · 9 hydrogen bonds · protein-protein
  • D–E · 935 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 182 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 144 Ų buried · 1 hydrogen bond · protein-protein
  • B–E · 84 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3JPU · LasR-TP4 complex · the same entry in another collection · chain E against E, TM-score 1.00
  • P25084 · AlphaFold monomer V2.0 prediction for transcriptional activator protein lasr (P25084) · a predicted model of the same protein · chain D against A, TM-score 0.99

Analyse

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