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MolNFT v1 · #183677 · protein

Crystal structure of mouse ADAT2/ADAT3 tRNA deamination complex V128L mutant

7NZ9 · TRNA-specific adenosine deaminase 2: “Crystal structure of mouse ADAT2/ADAT3 tRNA deamination complex V128L mutant”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.71). MolNFT v1 #183677 on GenesisL1: 3D structure…

PDB
7NZ9
Type
protein
Length
443 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA-specific adenosine deaminase 2; Probable inactive tRNA-specific adenosine…
EC
3.5.4.33
UniProt
Q6P6J0, Q6PAT0
Ligands
ZN
Pockets
4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATRNA-specific adenosine deaminase 2 (EC 3.5.4.33)protein16142% helix, 20% strandQ6P6J0
BProbable inactive tRNA-specific adenosine deaminase-like protein 3protein28229% helix, 23% strandQ6PAT0

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12180.710.8732empty
2760.500.8414empty
31210.410.7520empty
4770.350.7618empty

Interfaces

1 interface between chains.

  • A–B · 1255 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 7NZ9 · Crystal structure of mouse ADAT2/ADAT3 tRNA deamination complex V128L mutant · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6P6J0 · AlphaFold monomer V2.0 prediction for tRNA-specific adenosine deaminase 2 (Q6P6J0) · a predicted model of the same protein · chain A against A, TM-score 0.96
  • Q6PAT0 · AlphaFold monomer V2.0 prediction for probable inactive tRNA-specific adenosine… · a predicted model of the same protein · chain B against A, TM-score 0.63

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