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1.20 a resolution structure of the C-terminally truncated [2FE-2S] ferredoxin (bfd) from pseudomonas aeruginosa

Analyse 1.20 a resolution structure of the C-terminally truncated [2FE-2S] ferredoxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6E6Q
Type: protein
Length: 112 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacterioferritin-associated ferredoxin
UniProt: A0A069Q647
Ligands: FES
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bacterioferritin-associated ferredoxin	protein	56	54% helix, 9% strand	A0A069Q647

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.34	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 247 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6E6Q · 1.20 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd) from… · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A069Q647
Elsewhere: RCSB PDB 6E6Q · PDBe 6E6Q · UniProt A0A069Q647

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