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Crystal structure of RNA polymerase-associated protein RTF1 homolog plus-3 domain

Analyse Crystal structure of RNA polymerase-associated protein RTF1 homolog plus-3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3U1U
Type
protein
Length
260 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA polymerase-associated protein RTF1 homolog
UniProt
Q92541
Ligands
UNX, SO4
Pockets
3 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA polymerase-associated protein RTF1 homologprotein13134% helix, 36% strandQ92541
BRNA polymerase-associated protein RTF1 homologprotein12935% helix, 36% strandQ92541

Ligands and binding sites

  • UNX · Unknown atom or ion · ion · 23 copies · chains A, B
  • SO4 · Sulfate ion · ion · 4 copies · chains A, B
  • GOL · Glycerol · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11330.470.7818SO4
2850.350.7519SO4, UNX
3540.290.7515UNX

Interfaces

1 interface between chains.

  • A–B · 405 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 3U1U · Crystal structure of RNA polymerase-associated protein RTF1 homolog Plus-3 domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q92541 · AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein RTF1 homolog… · a predicted model of the same protein · chain B against A, TM-score 0.99

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