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Crystal structure of pyrococcus furiosus pbab, an archaeal proteasome activator

Analyse Crystal structure of pyrococcus furiosus pbab, an archaeal proteasome activator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VR0
Type
protein
Length
984 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative uncharacterized protein
UniProt
Q8U1R3
Ligands
AU
Pockets
12 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPutative uncharacterized proteinprotein24436% helix, 26% strandQ8U1R3
CPutative uncharacterized proteinprotein24834% helix, 26% strandQ8U1R3
DPutative uncharacterized proteinprotein24835% helix, 26% strandQ8U1R3

Ligands and binding sites

  • AU · Gold ion · metal · 18 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17540.690.7661AU
21200.500.8017empty
31230.470.7929AU
41020.460.7917empty
51180.440.7726AU

Interfaces

4 interfaces between chains.

  • A–D · 1241 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1211 Ų buried · 17 hydrogen bonds · protein-protein
  • B–C · 1191 Ų buried · 16 hydrogen bonds · protein-protein
  • C–D · 1125 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 3VR0 · Crystal structure of Pyrococcus furiosus PbaB, an archaeal proteasome activator · the same entry in another collection · chain A against A, TM-score 1.00

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