GL1X · GenesisL1 explorer

UniProt Q5SE95

Q5SE95

Q5SE95 (UniProt Q5SE95): 16 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q5SE95
Experimental structures
16
Predicted models
0

Structures

16 records of Q5SE95 in the MolNFT archive: 16 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
4B63A. fumigatus ornithine hydroxylase (SidA) bound to NADP and ornithinex-ray diffractionA——
4B63A. fumigatus ornithine hydroxylase (sida) bound to NADP and ornithinex-ray diffractionA——
4B64A. fumigatus ornithine hydroxylase (SidA) bound to NADP and Lysinex-ray diffractionA——
4B64A. fumigatus ornithine hydroxylase (sida) bound to NADP and lysinex-ray diffractionA——
4B65A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP(H)x-ray diffractionA——
4B65A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP(H)x-ray diffractionA——
4B66A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP and Argx-ray diffractionA——
4B66A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP and argx-ray diffractionA——
4B67A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and ornithinex-ray diffractionA——
4B67A. fumigatus ornithine hydroxylase (sida), re-oxidised state bound to NADP and ornithinex-ray diffractionA——
4B68A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and Argx-ray diffractionA——
4B68A. fumigatus ornithine hydroxylase (sida), re-oxidised state bound to NADP and argx-ray diffractionA——
4B69A. fumigatus ornithine hydroxylase (SidA) bound to ornithinex-ray diffractionA——
4B69A. fumigatus ornithine hydroxylase (sida) bound to ornithinex-ray diffractionA——
4NZHA. fumigatus flavin-dependent ornithine monooxygenase R279A mutantx-ray diffractionA——
4NZHA. fumigatus flavin-dependent ornithine monooxygenase R279A mutantx-ray diffractionA——

Elsewhere

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