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Crystal structures and thermostability of mutant TRAP3 A5 (engineered trap)

Analyse Crystal structures and thermostability of mutant TRAP3 A5 (engineered trap) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZD0
Type
protein
Length
195 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription attenuation protein mtrb
UniProt
Q9X6J6
Ligands
TRP
Pockets
3 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 61% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription attenuation protein mtrbprotein630% helix, 60% strandQ9X6J6
B, CTranscription attenuation protein mtrbprotein660% helix, 62% strandQ9X6J6

Ligands and binding sites

  • TRP · Tryptophan · ligand · 3 copies · chains A, B, C

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1820.740.9721TRP
2880.740.9718TRP
3760.420.7917empty

Interfaces

2 interfaces between chains.

  • B–C · 1033 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 913 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 2ZD0 · Crystal structures and thermostability of mutant TRAP3 A5 (ENGINEERED TRAP) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9X6J6 · AlphaFold monomer V2.0 prediction for transcription attenuation protein mtrb (Q9X6J6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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