GL1X · GenesisL1 explorer

Research workbench

Crystal structure of dmsp lyase rddddp from roseobacter denitrificans

Analyse Crystal structure of dmsp lyase rddddp from roseobacter denitrificans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4B28
Type
protein
Length
437 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Metallopeptidase, family M24, putative
UniProt
Q166H0
Ligands
FE
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMetallopeptidase, family M24, putativeprotein43739% helix, 19% strandQ166H0

Ligands and binding sites

  • FE · Fe (III) ion · metal · 2 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11170.590.8526empty

Compared structures

  • 4B28 · Crystal structure of DMSP lyase RdDddP from Roseobacter denitrificans · the same entry in another collection · chain A against A, TM-score 1.00
  • Q166H0 · AlphaFold monomer V2.0 prediction for dimethylsulfonioproprionate lyase dddp (Q166H0) · 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.