GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the dehydratase domain of mlnd from bacillus amyloliquefaciens

Analyse Crystal structure of the dehydratase domain of mlnd from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IL5
Type
protein
Length
510 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mlnd
UniProt
A7Z473
Pockets
7 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMlndprotein25319% helix, 37% strandA7Z473
BMlndprotein25718% helix, 36% strandA7Z473

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.610.9315empty
22360.610.8132empty
3760.550.8618empty
4710.450.8221empty
5520.410.8221empty

Interfaces

1 interface between chains.

  • A–B · 683 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 5IL5 · Crystal structure of the dehydratase domain of MlnD from Bacillus amyloliquefaciens · 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.