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Crystal structure of the bacterial proteasome activator bpa of mycobacterium tuberculosis (space group P3)

Analyse Crystal structure of the bacterial proteasome activator bpa of mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LFQ
Type
protein
Length
1,808 residues
Chains
16
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bacterial proteasome activator
UniProt
P9WKX3
Pockets
20 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, PBacterial proteasome activatorprotein11375% helix, 2% strandP9WKX3

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12540.580.7836empty
22790.570.7726empty
32240.560.7832empty
42190.550.7825empty
52110.540.7821empty

Interfaces

27 interfaces between chains.

  • G–H · 1153 Ų buried · 16 hydrogen bonds · protein-protein
  • O–P · 1153 Ų buried · 13 hydrogen bonds · protein-protein
  • I–J · 1150 Ų buried · 12 hydrogen bonds · protein-protein
  • B–G · 1140 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1136 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 48 modified (engineered).

Compared structures

  • 5LFQ · Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis… · the same entry in another collection · chain I against I, TM-score 1.00

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