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The crystal structure of the ferredoxin protease fusc E83A mutant in complex with arabidopsis ferredoxin

Analyse The crystal structure of the ferredoxin protease fusc E83A mutant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6B05
Type
protein
Length
944 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative zinc protease; Ferredoxin-2, chloroplastic
UniProt
Q6D8U3, P16972
Ligands
ZN
Pockets
10 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative zinc proteaseprotein89646% helix, 20% strandQ6D8U3
BFerredoxin-2, chloroplasticprotein4120% helix, 41% strandP16972
CFerredoxin-2, chloroplasticprotein70% helix, 0% strandP16972

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19910.840.85119empty
26050.660.7659empty
35440.620.7551empty
4960.540.8421empty
51530.480.7725empty

Interfaces

2 interfaces between chains.

  • A–B · 837 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 346 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6B05 · The Crystal Structure of the Ferredoxin Protease FusC E83A mutant in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P16972 · AlphaFold monomer V2.0 prediction for ferredoxin-2, chloroplastic (P16972) · a predicted model of the same protein · chain B against A, TM-score 0.85

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