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Cryo-EM structure of transmembrane aaa+ protease ftsh in the ADP state

Analyse Cryo-EM structure of transmembrane aaa+ protease ftsh in the ADP state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TDO
Type
protein
Length
2,520 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent zinc metalloprotease ftsh
EC
3.4.24.-
UniProt
Q9WZ49
Ligands
ADP
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 42% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-)protein42042% helix, 10% strandQ9WZ49

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110410.750.78104empty
210410.750.78102ADP
39500.740.78109empty
410990.740.77106ADP
58160.730.7893empty

Interfaces

6 interfaces between chains.

  • D–F · 2125 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 2076 Ų buried · 21 hydrogen bonds · protein-protein
  • A–E · 1994 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 1983 Ų buried · 16 hydrogen bonds · protein-protein
  • C–D · 1980 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 7TDO · Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state · the same entry in another collection · chain F against F, TM-score 1.00
  • Q9WZ49 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (Q9WZ49) · a predicted model of the same protein · chain C against A, TM-score 0.88

Analyse

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