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MolNFT v1 · #149862 · protein

Truncated ftsh from a. aeolicus in P312

6GCO · ATP-dependent zinc metalloprotease ftsh: “Truncated ftsh from a. aeolicus in P312”. X-ray diffraction, 2 ligands (ADP, ZN), 12 pockets (best druggability 0.74). MolNFT v1 #149862 on GenesisL1: 3D structure, binding sites and pockets…

PDB
6GCO
Type
protein
Length
804 residues
Chains
2
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
Pockets
12 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-)protein40957% helix, 8% strandO67077
BATP-dependent zinc metalloprotease ftsh (EC 3.4.24.-)protein39560% helix, 7% strandO67077

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16070.740.8171empty
22940.740.8741empty
35510.730.8185ADP
44660.730.8262ADP
52050.640.8335empty

Interfaces

1 interface between chains.

  • A–B · 942 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6GCO · Truncated FtsH from A. aeolicus in P312 · 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 A against A, TM-score 0.60

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