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Complex structure of afcca with trnaminidcg

Analyse Complex structure of afcca with trnaminidcg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZH4
Type
protein + RNA
Length
471 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cca-adding enzyme; TRNA (34-mer)
EC
2.7.7.25, 2.7.7.21
UniProt
O28126
Ligands
SO4
Pockets
6 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACca-adding enzyme (EC 2.7.7.25, 2.7.7.21)protein43745% helix, 22% strandO28126
BTRNA (34-mer)rna34——

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15400.670.7861SO4
26170.620.7449empty
34660.550.7329SO4
43820.540.7431empty
5540.330.7712empty

Interfaces

1 interface between chains.

  • A–B · 1459 Ų buried · 36 hydrogen bonds · protein-nucleic

Compared structures

  • 2ZH4 · Complex structure of AFCCA with tRNAminiDCG · the same entry in another collection · chain A against A, TM-score 1.00
  • O28126 · AlphaFold monomer V2.0 prediction for cca-adding enzyme (O28126) · a predicted model of the same protein · chain A against A, TM-score 0.98

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