GL1X · GenesisL1 explorer

MolNFT v1 · #127165 · protein

Ethylene forming enzyme from pseudomonas syringae pv. phaseolicola - I222 crystal form in complex with manganese and 2-oxoglutarate

5MOF · 2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming enzyme: “Ethylene forming enzyme from pseudomonas syringae pv. phaseolicola - I222 crystal form in complex with…”. X-ray diffraction, 3 ligands (AKG, MN, CL), 2 pockets (best…

PDB
5MOF
Type
protein
Length
343 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming enzyme
EC
1.13.12.19, 1.14.11.34
UniProt
P32021
Ligands
AKG, MN, CL
Pockets
2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming enzyme (EC 1.13.12.19, 1.14.11.34)protein34331% helix, 19% strandP32021

Ligands and binding sites

  • AKG · 2-oxoglutaric acid · ligand · 2 copies · chains A
  • MN · Manganese (II) ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14120.760.8565MN, CL, AKG
21410.440.7620empty

Compared structures

  • 5MOF · Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - I222 crystal form in… · the same entry in another collection · chain A against A, TM-score 1.00
  • P32021 · AlphaFold monomer V2.0 prediction for 2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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