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MolNFT v1 · #112036 · protein

Truncated ftsh from a. aeolicus

4Z8X · ATP-dependent zinc metalloprotease ftsh: “Truncated ftsh from a. aeolicus”. X-ray diffraction, 3 ligands (ADP, ZN, SO4), 16 pockets (best druggability 0.72). MolNFT v1 #112036 on GenesisL1: 3D structure, binding sites and pockets in…

PDB
4Z8X
Type
protein
Length
1,273 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent zinc metalloprotease ftsh
EC
3.4.24.-
UniProt
O67077
Ligands
ADP, ZN, SO4
Pockets
16 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-)protein42552% helix, 9% strandO67077
CATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-)protein42353% helix, 8% strandO67077

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, C
  • ZN · Zinc ion · metal · 3 copies · chains A, B, C
  • SO4 · Sulfate ion · ion · 3 copies · chains A, C, B

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

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110540.720.76105ADP
28460.700.76103ZN, ADP
31150.690.9121empty
47360.690.7681empty
5670.690.9417empty

Interfaces

2 interfaces between chains.

  • A–B · 1607 Ų buried · 21 hydrogen bonds · protein-protein
  • A–C · 1547 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 4Z8X · Truncated FtsH from A. aeolicus · the same entry in another collection · chain A against A, TM-score 1.00
  • O67077 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (O67077) · a predicted model of the same protein · chain B against A, TM-score 0.62

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