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UniProt P11073

P11073

P11073 (UniProt P11073): 31 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P11073
Experimental structures
31
Predicted models
0

Structures

31 records of P11073 in the MolNFT archive: 31 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1AIRPectate lyase C from erwinia chrysanthemi (EC16) to a resolution of 2.2 ångströms with 128 watersx-ray diffractionA——
1AIRPectate lyase C from erwinia chrysanthemi (EC16) to a resolution of 2.2 ångströms with 128 watersx-ray diffractionA——
1O88Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 30mM Ca2+x-ray diffractionA——
1O88Pectate lyase C from erwinia chrysanthemi at pH 11.2 with 30MM CA2+x-ray diffractionA——
1O8DPectate Lyase C from Erwinia Chrysanthemi at pH 11.2 with 5mM CA2+x-ray diffractionA——
1O8DPectate lyase C from erwinia chrysanthemi at pH 11.2 with 5MM CA2+x-ray diffractionA——
1O8EPectate Lyase C from Erwinia Chrysanthemi at pH 11.2 with 1mM Ca2+x-ray diffractionA——
1O8EPectate lyase C from erwinia chrysanthemi at pH 11.2 with 1MM CA2+x-ray diffractionA——
1O8FPectate Lyase C from Erwinia Chrysanthemi at pH 9.5 with 30mM Ca2+x-ray diffractionA——
1O8FPectate lyase C from erwinia chrysanthemi at pH 9.5 with 30MM CA2+x-ray diffractionA——
1O8GPectate Lyase C from Erwinia Chrysanthemi at pH 9.5 with 5mM Ca2+x-ray diffractionA——
1O8GPectate lyase C from erwinia chrysanthemi at pH 9.5 with 5MM CA2+x-ray diffractionA——
1O8HPectate Lyase C from Erwinia Chrysanthemi at pH 9.5 with 0.3mM Ca2+ Addedx-ray diffractionA——
1O8HPectate lyase C from erwinia chrysanthemi at pH 9.5 with 0.3MM CA2+ addedx-ray diffractionA——
1O8IPectate Lyase C from Erwinia Chrysanthemi at pH 9.5 with no Ca2+ Addedx-ray diffractionA——
1O8IPectate lyase C from erwinia chrysanthemi at pH 9.5 with no CA2+ addedx-ray diffractionA——
1O8JPectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with 30mM CA2+x-ray diffractionA——
1O8JPectate lyase C from erwinia chrysanthemi at pH 4.5 with 30MM CA2+x-ray diffractionA——
1O8KPectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with 20mM CA2+x-ray diffractionA——
1O8KPectate lyase C from erwinia chrysanthemi at pH 4.5 with 20MM CA2+x-ray diffractionA——
1O8LPectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with 5mM CA2+x-ray diffractionA——
1O8LPectate lyase C from erwinia chrysanthemi at pH 4.5 with 5MM CA2+x-ray diffractionA——
1O8MPectate Lyase C from Erwinia Chrysanthemi at pH 4.5 with no Ca2+ Addedx-ray diffractionA——
1O8MPectate lyase C from erwinia chrysanthemi at pH 4.5 with no CA2+ addedx-ray diffractionA——
1PLUPectate lyase C from erwinia chrysanthemi with 1 LU+3 ion in the putative calcium binding sitex-ray diffractionA——
1PLUPectate lyase C from erwinia chrysanthemi with 1 LU+3 ion in the putative calcium binding sitex-ray diffractionA——
2EWECrystal structure of Pectate Lyase C R218K mutant in complex with pentagalacturonic acidx-ray diffractionA——
2EWECrystal structure of pectate lyase C R218K mutant in complex with pentagalacturonic acidx-ray diffractionA——
2PECThe refined three-dimensional structure of pectate lyase C from erwinia chrysanthemi at 2.2…x-ray diffractionA——
2PECThe refined three-dimensional structure of pectate lyase C from erwinia chrysanthemi at 2.2…x-ray diffractionA——
P11073AlphaFold monomer V2.0 prediction for pectate lyase C (P11073)———

Elsewhere

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