GL1X · GenesisL1 explorer

Research workbench

The crystal structure of SMU.143C from streptococcus mutans UA159

Analyse The crystal structure of SMU.143C from streptococcus mutans UA159 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3L87
Type
protein
Length
200 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptide deformylase
EC
3.5.1.88
UniProt
Q8DWC2
Ligands
FE
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptide deformylase (EC 3.5.1.88)protein20028% helix, 25% strandQ8DWC2

Ligands and binding sites

  • FE · Fe (III) ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11250.500.8020empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 3L87 · The Crystal Structure of smu.143c from Streptococcus mutans UA159 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8DWC2 · AlphaFold monomer V2.0 prediction for peptide deformylase (Q8DWC2) · a predicted model of the same protein · 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.