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UniProt P00924

P00924

P00924 (UniProt P00924): 40 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P00924
Experimental structures
40
Predicted models
1
Ligands
4

Structures

41 records of P00924 in the MolNFT archive: 40 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1EBGChelation of ser 39 to MG2+ latches a gate at the active site of enolase: structure of the…x-ray diffractionA, B——
1EBGChelation of ser 39 to MG2+ latches a gate at the active site of enolase: structure of the…x-ray diffractionA, B——
1EBHOctahedral coordination at the high affinity metal site in enolase; crystallographic analysis of…x-ray diffractionA, B——
1EBHOctahedral coordination at the high affinity metal site in enolase; crystallographic analysis of…x-ray diffractionA, B——
1ELSCatalytic metal ion binding in enolase: the crystal structure of…x-ray diffractionA——
1ELSCatalytic metal ion binding in enolase: the crystal structure of…x-ray diffractionA——
1L8PMg-phosphonoacetohydroxamate complex of S39A yeast enolase 1x-ray diffractionA, B, C, D——
1L8PMg-phosphonoacetohydroxamate complex of S39A yeast enolase 1x-ray diffractionA, B, C, D——
1NELFluoride inhibition of yeast enolase: crystal structure of the enolase-MG2+-F--pi complex at…x-ray diffractionA——
1NELFluoride inhibition of yeast enolase: crystal structure of the enolase-MG2+-F--pi complex at…x-ray diffractionA——
1ONEYeast enolase complexed with an equilibrium mixture of 2'-phosphoglyceate and phosphoenolpyruvatex-ray diffractionA, B——
1ONEYeast enolase complexed with an equilibrium mixture of 2'- phosphoglyceate and phosphoenolpyruvatex-ray diffractionA, B——
1P43Reverse protonation is the key to general acid-base catalysis in enolasex-ray diffractionA, B——
1P43Reverse protonation is the key to general acid-base catalysis in enolasex-ray diffractionA, B——
1P48Reverse protonation is the key to general acid-base catalysis in enolasex-ray diffractionA, B——
1P48Reverse protonation is the key to general acid-base catalysis in enolasex-ray diffractionA, B——
2AL1Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0x-ray diffractionA, B——
2AL1Crystal structure analysis of enolase mg subunit complex at pH 8.0x-ray diffractionA, B——
2AL2Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0x-ray diffractionA, B——
2AL2Crystal structure analysis of enolase mg subunit complex at pH 8.0x-ray diffractionA, B——
2ONEAsymmetric yeast enolase dimer complexed with resolved 2'-phosphoglycerate and phosphoenolpyruvatex-ray diffractionA, B——
2ONEAsymmetric yeast enolase dimer complexed with resolved 2'- phosphoglycerate and phosphoenolpyruvatex-ray diffractionA, B——
2XGZEngineering the enolase active site pocket: Crystal structure of the S39N D321R mutant of yeast…x-ray diffractionA, B——
2XGZEngineering the enolase active site pocket: crystal structure of the S39N D321R mutant of yeast…x-ray diffractionA, B——
2XH0Engineering the enolase active site pocket: Crystal structure of the S39N Q167K D321R mutant of…x-ray diffractionA, B, C, D——
2XH0Engineering the enolase active site pocket: crystal structure of the S39N Q167K D321R mutant of…x-ray diffractionA, B, C, D——
2XH2Engineering the enolase active site pocket: Crystal structure of the S39N D321A mutant of yeast…x-ray diffractionA, B, C, D——
2XH2Engineering the enolase active site pocket: crystal structure of the S39N D321A mutant of yeast…x-ray diffractionA, B, C, D——
2XH4Engineering the enolase active site pocket: Crystal structure of the S39A D321A mutant of yeast…x-ray diffractionA, B, C, D——
2XH4Engineering the enolase active site pocket: crystal structure of the S39A D321A mutant of yeast…x-ray diffractionA, B, C, D——
2XH7Engineering the enolase active site pocket: Crystal structure of the D321A mutant of yeast enolase 1x-ray diffractionA, B——
2XH7Engineering the enolase active site pocket: crystal structure of the D321A mutant of yeast enolase 1x-ray diffractionA, B——
3ENLRefined structure of yeast apo-enolase at 2.25 ångströms resolutionx-ray diffractionA——
3ENLRefined structure of yeast apo-enolase at 2.25 ångströms resolutionx-ray diffractionA——
4ENLCrystal structure of holoenzyme refined at 1.9 ångströms resolution: trigonal-bipyramidal geometry…x-ray diffractionA——
4ENLCrystal structure of holoenzyme refined at 1.9 ångströms resolution: trigonal-bipyramidal geometry…x-ray diffractionA——
5ENLInhibition of enolase: the crystal structures of enolase-CA2+- phosphoglycerate and…x-ray diffractionA——
6ENLInhibition of enolase: the crystal structures of enolase-CA2+- phosphoglycerate and…x-ray diffractionAPGA, ZN—
7ENLMechanism of enolase: the crystal structure of enolase-MG2+-PHOSPHOGLYCERATE(SLASH)…x-ray diffractionAMG, 2PG—
7ENLMechanism of enolase: the crystal structure of enolase-MG2+- PHOSPHOGLYCERATE(SLASH)…x-ray diffractionAMG, 2PG—
P00924AlphaFold monomer V2.0 prediction for enolase 1 (P00924)predictedA——

Ligands

  • 2PG · 2-phosphoglyceric acid · in 2 records
  • MG · Magnesium ion · in 2 records
  • PGA · 2-phosphoglycolic acid · in 1 record
  • ZN · Zinc ion · in 1 record

Experiment against prediction

Elsewhere

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