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Crystal structure of the 2FE 2S ferredoxin from cyanidioschyzon merolae

Analyse Crystal structure of the 2FE 2S ferredoxin from cyanidioschyzon merolae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AB5
Type
protein
Length
194 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferredoxin
UniProt
Q85FT5
Ligands
FES
Pockets
1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BFerredoxinprotein9720% helix, 32% strandQ85FT5

Ligands and binding sites

  • FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.410.7721empty

Interfaces

1 interface between chains.

  • A–B · 321 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3AB5 · Crystal structure of the 2Fe 2S Ferredoxin from Cyanidioschyzon merolae · the same entry in another collection · chain A against A, TM-score 1.00

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