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Crystal structure of the PED208 tram-sbma complex

Analyse Crystal structure of the PED208 tram-sbma complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ON0
Type
protein + DNA
Length
488 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein tram; Sbma
UniProt
P33788
Pockets
3 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 76% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein tramprotein12175% helix, 4% strandP33788
B, CProtein tramprotein11876% helix, 4% strandP33788
DProtein tramprotein10777% helix, 5% strandP33788
PSbmadna24——

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1950.760.9820empty
21510.650.8720empty
33030.600.7835empty

Interfaces

10 interfaces between chains.

  • B–C · 2974 Ų buried · 26 hydrogen bonds · protein-protein
  • A–D · 2870 Ų buried · 25 hydrogen bonds · protein-protein
  • A–C · 1398 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 1304 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 651 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3ON0 · Crystal structure of the pED208 TraM-sbmA complex · the same entry in another collection · chain P against P, TM-score 1.00
  • P33788 · AlphaFold monomer V2.0 prediction for relaxosome protein tram (P33788) · a predicted model of the same protein · chain D against A, TM-score 0.54

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