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1.50 angstroem crystal structure of feoa from bacteroides fragilis

Analyse 1.50 angstroem crystal structure of feoa from bacteroides fragilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7R7B
Type
protein
Length
148 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferrous iron transport protein B
UniProt
A0A081U6Q6
Ligands
PO4
Pockets
1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BFerrous iron transport protein Bprotein7423% helix, 39% strandA0A081U6Q6

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A, B
  • GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.600.8038GOL

Interfaces

1 interface between chains.

  • A–B · 238 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 7R7B · 1.50 Angstroem Crystal Structure of FeoA from Bacteroides fragilis · the same entry in another collection · chain A against A, TM-score 1.00

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