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MolNFT v1 · #32665 · protein

Crystal structure of B.SUBTILIS anti-trap protein, an antagonist of trap-RNA interactions

2BX9 · Tryptophan RNA-binding attenuator protein-inhibitory protein: “Crystal structure of B.SUBTILIS anti-trap protein, an antagonist of trap-RNA interactions”. X-ray diffraction, 1 ligand (ZN), 12 pockets (best druggability 0.80). MolNFT…

PDB
2BX9
Type
protein
Length
636 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophan RNA-binding attenuator protein-inhibitory protein
UniProt
O31466
Ligands
ZN
Pockets
12 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LTryptophan RNA-binding attenuator protein-inhibitory proteinprotein5332% helix, 19% strandO31466

Ligands and binding sites

  • ZN · Zinc ion · metal · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L

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

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13500.800.9034empty
2500.660.9617empty
3520.640.9418empty
4840.410.7823empty
5930.370.7524empty

Interfaces

34 interfaces between chains.

  • A–B · 699 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 698 Ų buried · 8 hydrogen bonds · protein-protein
  • D–E · 692 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 691 Ų buried · 6 hydrogen bonds · protein-protein
  • D–F · 676 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 2BX9 · Crystal structure of B.subtilis Anti-TRAP protein, an antagonist of TRAP-RNA interactions · the same entry in another collection · chain L against L, TM-score 1.00

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