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R381K mutant of flavocytochrome C3

Analyse R381K mutant of flavocytochrome C3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2B7S
Type
protein
Length
568 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fumarate reductase flavoprotein subunit
EC
1.3.99.1
UniProt
Q02469
Ligands
HEM, FAD, FUM, NA
Pockets
5 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFumarate reductase flavoprotein subunit (EC 1.3.99.1)protein56836% helix, 18% strandQ02469

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A
  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • FUM · Fumaric acid · ligand · chains A
  • NA · Sodium ion · metal · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16590.840.8993HEM, FAD, FUM
29040.780.8189HEM
3850.370.7619empty
4700.370.7823empty
5770.320.7421empty

Modifications

Observed in the structure: 6 cofactor (heme attachment).

Compared structures

  • 2B7S · R381K mutant of flavocytochrome c3 · the same entry in another collection · chain A against A, TM-score 1.00

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