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MolNFT v1 · #80232 · protein

Structure of an ribosomal subunit interface protein from coxiella burnetii

3TQM · Ribosome-associated factor Y: “Structure of an ribosomal subunit interface protein from coxiella burnetii”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.78). MolNFT v1 #80232 on GenesisL1: 3D structure, binding…

PDB
3TQM
Type
protein
Length
369 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribosome-associated factor Y
UniProt
Q83DI6
Ligands
SO4
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosome-associated factor Yprotein9137% helix, 36% strandQ83DI6
BRibosome-associated factor Yprotein9238% helix, 36% strandQ83DI6
C, DRibosome-associated factor Yprotein9338% helix, 38% strandQ83DI6

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D

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
110920.780.80111empty
21200.510.8123empty
31120.480.8025empty

Interfaces

5 interfaces between chains.

  • A–C · 526 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 525 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 214 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 213 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 146 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 3TQM · Structure of an ribosomal subunit interface protein from Coxiella burnetii · the same entry in another collection · chain C against C, TM-score 1.00

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