GL1X · GenesisL1 explorer

Research workbench

Structure of the substrate-free FAD-dependent tirandamycin oxidase taml

Analyse Structure of the substrate-free FAD-dependent tirandamycin oxidase taml in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y08
Type
protein
Length
998 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Taml
UniProt
D3Y1I2
Ligands
FAD, MG, CL
Pockets
10 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATamlprotein49833% helix, 21% strandD3Y1I2
BTamlprotein50032% helix, 21% strandD3Y1I2

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · 8 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13700.840.9370FAD, GOL
24090.840.9280MG, CL
32890.830.9452FAD
41270.760.9542MG
5840.600.8819empty

Interfaces

1 interface between chains.

  • A–B · 1815 Ų buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (flavinylation).

Compared structures

  • 2Y08 · Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.