GL1X · GenesisL1 explorer

UniProt Q27709

Obelin (Q27709)

Obelin (UniProt Q27709): 31 experimental structures on GenesisL1, 5 ligands bound, 9 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q27709
Protein
Obelin
Experimental structures
31
Predicted models
0
Ligands
5
Pockets
9 · 3 records with a druggable one

Structures

31 records of Q27709 in the MolNFT archive: 31 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1EL4Structure of the calcium-regulated photoprotein obelin determined by sulfur sasx-ray diffractionA——
1EL4Structure of the calcium-regulated photoprotein obelin determined by sulfur sasx-ray diffractionA——
1JF0The Crystal Structure of Obelin from Obelia geniculata at 1.82 A Resolutionx-ray diffractionA——
1JF0The crystal structure of obelin from obelia geniculata at 1.82 a resolutionx-ray diffractionA——
1JF2Crystal Structure of W92F obelin mutant from Obelia longissima at 1.72 Angstrom resolutionx-ray diffractionA——
1JF2Crystal structure of W92F obelin mutant from obelia longissima at 1.72 ångström resolutionx-ray diffractionA——
1QV0Atomic resolution structure of obelin from Obelia longissimax-ray diffractionA——
1QV0Atomic resolution structure of obelin from obelia longissimax-ray diffractionA——
1QV1Atomic resolution structure of obelin from Obelia longissimax-ray diffractionA——
1QV1Atomic resolution structure of obelin from obelia longissimax-ray diffractionA——
1S36Crystal structure of a Ca2+-discharged photoprotein: Implications for the mechanisms of the calcium…x-ray diffractionA——
1S36Crystal structure of a CA2+-discharged photoprotein: implications for the mechanisms of the calcium…x-ray diffractionA——
1SL7Crystal structure of calcium-loaded apo-obelin from Obelia longissimax-ray diffractionA——
1SL7Crystal structure of calcium-loaded apo-obelin from obelia longissimax-ray diffractionA——
1SL9Obelin from Obelia longissimax-ray diffractionA——
1SL9Obelin from obelia longissimax-ray diffractionA——
2F8PCrystal structure of obelin following Ca2+ triggered bioluminescence suggests neutral…x-ray diffractionA——
2F8PCrystal structure of obelin following CA2+ triggered bioluminescence suggests neutral…x-ray diffractionA——
4MRXCrystal Structure of Y138F obelin mutant from Obelia longissima at 1.72 Angstrom resolutionx-ray diffractionA——
4MRXCrystal structure of Y138F obelin mutant from obelia longissima at 1.72 ångström resolutionx-ray diffractionA——
4MRYCrystal Structure of Ca(2+)- discharged Y138F obelin mutant from Obelia longissima at 1.30 Angstrom…x-ray diffractionA——
4MRYCrystal structure of CA(2+)- discharged Y138F obelin mutant from obelia longissima at 1.30 ångström…x-ray diffractionA——
4N1FCrystal Structure of F88Y obelin mutant from Obelia longissima at 2.09 Angstrom resolutionx-ray diffractionA——
4N1FCrystal structure of F88Y obelin mutant from obelia longissima at 2.09 ångström resolutionx-ray diffractionA——
4N1GCrystal Structure of Ca(2+)- discharged F88Y obelin mutant from Obelia longissima at 1.50 Angstrom…x-ray diffractionA, B——
4N1GCrystal structure of CA(2+)- discharged F88Y obelin mutant from obelia longissima at 1.50 ångström…x-ray diffractionA, B——
7O3UThe crystal structure of obelin from Obelia longissima bound with v-coelenterazinex-ray diffractionAV1W, CA1 (best 0.83)
7O3UThe crystal structure of obelin from obelia longissima bound with V- coelenterazinex-ray diffractionAV1W, CA—
8A9SCrystal structure of Ca2+-discharged obelin in complex with coelenteramine-vx-ray diffractionA, BLK9, NA4 (best 0.83)
8C6OCrystal Structure of H64F obelin mutant from Obelia longissima at 2.2 Angstrom resolutionx-ray diffractionA, BCZH, NA4 (best 0.84)
Q27709AlphaFold monomer V2.0 prediction for obelin (Q27709)———

Ligands

  • CA · Calcium ion · in 2 records
  • NA · Sodium ion · in 2 records
  • V1W · v-coelenterazine · in 2 records
  • CZH · C2-hydroperoxy-coelenterazine · in 1 record
  • LK9 · 3-azanyl-2-(phenylmethyl)benzo[f]quinoxalin-8-ol · in 1 record

Elsewhere

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