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Crystal structure of RTT109 from aspergillus fumigatus

Analyse Crystal structure of RTT109 from aspergillus fumigatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZB9
Type
protein
Length
402 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA damage response protein RTT109, putative
UniProt
Q4WUS9
Pockets
7 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA damage response protein RTT109, putativeprotein40230% helix, 21% strandQ4WUS9

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1760.740.9724empty
23000.670.8241GOL
31740.450.7526empty
4760.380.7819empty
5680.360.7718empty

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 5ZB9 · Crystal structure of Rtt109 from Aspergillus fumigatus · the same entry in another collection · chain A against A, TM-score 1.00

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