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Ethylene forming enzyme in complex with manganese, 2-oxoglutarate and N-omega-hydroxy-L-arginine

Analyse Ethylene forming enzyme in complex with manganese, 2-oxoglutarate and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VKA
Type
protein
Length
348 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.169
Source
Pseudomonas savastanoi pv. phaseolicola
Molecule
2-oxoglutarate-dependent ethylene/succinate-forming enzyme
EC
1.13.12.19, 1.14.11.34
UniProt
P32021
Ligands
AKG, HAR, MN
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · resolution 1.169 · 1 distinct chain · 33% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A2-oxoglutarate-dependent ethylene/succinate-forming enzyme (EC 1.13.12.19, 1.14.11.34)protein34833% helix, 19% strandP32021

Ligands and binding sites

  • AKG · 2-oxoglutaric acid · ligand · chains A
  • HAR · N-omega-hydroxy-L-arginine · ligand · chains A
  • MN · Manganese (II) ion · metal · 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
1830.740.9727MN, AKG
21020.380.7517empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 5VKA · Ethylene forming enzyme in complex with manganese, 2-oxoglutarate and… · 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 0.97

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