Research workbench

[2FE-2S]-ferredoxin from halobacterium salinarum

Analyse [2FE-2S]-ferredoxin from halobacterium salinarum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E0Z
Type: protein
Length: 128 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin
UniProt: P00216
Ligands: FES

Structure

solution nmr · 1 distinct chain · 28% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin	protein	128	28% helix, 19% strand	P00216

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · chains A

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

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

1E0Z · [2Fe-2S]-Ferredoxin from Halobacterium salinarum · the same entry in another collection · chain A against A, TM-score 1.00
P00216 · AlphaFold monomer V2.0 prediction for ferredoxin (P00216) · a predicted model of the same protein · chain A against A, TM-score 0.87

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00216
Elsewhere: RCSB PDB 1E0Z · PDBe 1E0Z · UniProt P00216

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