GL1X · GenesisL1 explorer

Research workbench

Catalytic domain from trimeric dihydrolipoamide succinyltransferase

Analyse Catalytic domain from trimeric dihydrolipoamide succinyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1C4T
Type
protein
Length
667 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (dihydrolipoamide succinyltransferase)
EC
2.3.1.61
UniProt
P07016
Ligands
SO4
Pockets
9 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (dihydrolipoamide succinyltransferase) (EC 2.3.1.61)protein22637% helix, 28% strandP07016
BProtein (dihydrolipoamide succinyltransferase) (EC 2.3.1.61)protein21740% helix, 26% strandP07016
CProtein (dihydrolipoamide succinyltransferase) (EC 2.3.1.61)protein22435% helix, 27% strandP07016

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 6 copies · chains A, C, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11130.790.9720empty
27660.750.8076SO4
35770.710.8064SO4
44030.690.8146SO4
5600.660.9419empty

Interfaces

3 interfaces between chains.

  • A–C · 1507 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 1360 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 1275 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 1C4T · Catalytic domain from trimeric dihydrolipoamide succinyltransferase · 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.