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MolNFT v1 · #178401 · protein

Cryo-EM structure of apo bsclpp at pH 4.2

7FES · ATP-dependent clp protease proteolytic subunit: “Cryo-EM structure of apo bsclpp at pH 4.2”. Electron microscopy, 20 pockets (best druggability 0.77). MolNFT v1 #178401 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7FES
Type
protein
Length
2,198 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 0.77

Structure

electron microscopy · 1 distinct chain · 41% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, NATP-dependent clp protease proteolytic subunit (EC 3.4.21.92)protein15741% helix, 4% strandP80244

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11570.770.9436empty
24430.770.8581empty
35820.760.8290empty
41170.740.9335empty
51350.730.9239empty

Interfaces

28 interfaces between chains.

  • K–L · 851 Ų buried · 1 hydrogen bond · protein-protein
  • H–N · 788 Ų buried · 1 hydrogen bond · protein-protein
  • J–K · 782 Ų buried · 2 hydrogen bonds · protein-protein
  • E–F · 780 Ų buried · 6 hydrogen bonds · protein-protein
  • A–G · 764 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7FES · Cryo-EM structure of apo BsClpP at pH 4.2 · the same entry in another collection · chain J against J, TM-score 1.00

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