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Cryo-EM structure of apo bsclpp at pH 6.5

Analyse Cryo-EM structure of apo bsclpp at pH 6.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7FEQ
Type
protein
Length
2,520 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent clp protease proteolytic subunit
EC
3.4.21.92
UniProt
P80244
Pockets
20 · best druggability 0.65

Structure

electron microscopy · 1 distinct chain · 34% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, I, J, K, L, M, N, HATP-dependent clp protease proteolytic subunit (EC 3.4.21.92)protein18034% helix, 17% strandP80244

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11020.650.9023empty
21070.640.8922empty
3870.640.9020empty
41120.640.8825empty
51060.630.8822empty

Interfaces

35 interfaces between chains.

  • D–E · 1319 Ų buried · 4 hydrogen bonds · protein-protein
  • K–L · 1301 Ų buried · 5 hydrogen bonds · protein-protein
  • A–G · 1298 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 1291 Ų buried · 8 hydrogen bonds · protein-protein
  • F–G · 1283 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7FEQ · Cryo-EM structure of apo BsClpP at pH 6.5 · the same entry in another collection · chain L against L, TM-score 1.00

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