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Crystal structure of EC1530, a putative oxygenase from escherichia COLI

Analyse Crystal structure of EC1530, a putative oxygenase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1K77
Type
protein
Length
260 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein ygbm
UniProt
Q46891
Ligands
MG
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical protein ygbmprotein26042% helix, 14% strandQ46891

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A
  • FMT · Formic acid · additive · 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
1960.440.7921GOL, FMT

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 1K77 · Crystal Structure of EC1530, a Putative Oxygenase from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
  • Q46891 · AlphaFold monomer V2.0 prediction for 2-oxo-tetronate isomerase (Q46891) · a predicted model of the same protein · chain A against A, TM-score 0.99

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