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Crystal structure of an archaeal pentameric riboflavin synthase

Analyse Crystal structure of an archaeal pentameric riboflavin synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2B98
Type
protein
Length
726 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Riboflavin synthase
EC
2.5.1.9
UniProt
Q58584
Pockets
9 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 54% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARiboflavin synthase (EC 2.5.1.9)protein14156% helix, 18% strandQ58584
BRiboflavin synthase (EC 2.5.1.9)protein14155% helix, 18% strandQ58584
C, ERiboflavin synthase (EC 2.5.1.9)protein15250% helix, 16% strandQ58584
DRiboflavin synthase (EC 2.5.1.9)protein14054% helix, 18% strandQ58584

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17850.850.88111empty
22800.770.8940empty
32280.690.8637empty
42020.680.8632empty
51110.410.7620empty

Interfaces

5 interfaces between chains.

  • C–D · 1324 Ų buried · 18 hydrogen bonds · protein-protein
  • C–E · 1322 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 1187 Ų buried · 12 hydrogen bonds · protein-protein
  • A–E · 1158 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 1149 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 2B98 · Crystal Structure of an archaeal pentameric riboflavin synthase · the same entry in another collection · chain D against D, TM-score 1.00
  • Q58584 · AlphaFold monomer V2.0 prediction for riboflavin synthase (Q58584) · a predicted model of the same protein · chain D against A, TM-score 0.99

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