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UniProt P03051

P03051

P03051 (UniProt P03051): 38 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P03051
Experimental structures
38
Predicted models
0

Structures

38 records of P03051 in the MolNFT archive: 38 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1B6QAlanine 31 proline mutant of rop proteinx-ray diffractionA——
1B6QAlanine 31 proline mutant of rop proteinx-ray diffractionA——
1F4MP3(2) crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core and a new…x-ray diffractionA, B, C, D, E, F——
1F4MP3(2) crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core and a new…x-ray diffractionA, B, C, D, E, F——
1F4NC2 crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core and a new…x-ray diffractionA, B——
1F4NC2 crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core and a new…x-ray diffractionA, B——
1GMGAlanine 31 proline mutant of rop protein, monoclinic formx-ray diffractionA, B——
1GMGAlanine 31 proline mutant of rop protein, monoclinic formx-ray diffractionA, B——
1GTOHigh resolution structure of a hyperstable helical bundle protein mutantx-ray diffractionA, B, C——
1GTOHigh resolution structure of a hyperstable helical bundle protein mutantx-ray diffractionA, B, C——
1NKDAtomic resolution (1.07 ångströms) structure of the rop mutant <2AA>x-ray diffractionA——
1NKDAtomic resolution (1.07 ångströms) structure of the rop mutant <2AA>x-ray diffractionA——
1QX8Crystal structure of a five-residue deletion mutant of the Rop proteinx-ray diffractionA, B——
1QX8Crystal structure of a five-residue deletion mutant of the rop proteinx-ray diffractionA, B——
1ROPStructure of the COL*E1 rop protein at 1.7 ångströms resolutionx-ray diffractionA——
1ROPStructure of the COL*E1 rop protein at 1.7 ångströms resolutionx-ray diffractionA——
1RPORestored heptad pattern continuity does not alter the folding of a 4-alpha-helical bundlex-ray diffractionA——
1RPORestored heptad pattern continuity does not alter the folding of a 4- alpha-helical bundlex-ray diffractionA——
1RPRThe structure of COLE1 rop in solutionsolution nmrA, B——
1RPRThe structure of COLE1 rop in solutionsolution nmrA, B——
1YO7Re-engineering topology of the homodimeric ROP protein into a single-chain 4-helix bundlex-ray diffractionA, B——
1YO7Re-engineering topology of the homodimeric rop protein into a single- chain 4-helix bundlex-ray diffractionA, B——
2GHYNovel Crystal Form of the ColE1 Rom Proteinx-ray diffractionA, B——
2GHYNovel crystal form of the COLE1 rom proteinx-ray diffractionA, B——
2IJHCrystal structure analysis of ColE1 ROM mutant F14Wx-ray diffractionA, B, C——
2IJHCrystal structure analysis of COLE1 rom mutant F14Wx-ray diffractionA, B, C——
2IJIStructure of F14H mutant of ColE1 Rom proteinx-ray diffractionA——
2IJIStructure of F14H mutant of COLE1 rom proteinx-ray diffractionA——
2IJJCrystal structure analysis of ColE1 ROM mutant F14Yx-ray diffractionA, B, C——
2IJJCrystal structure analysis of COLE1 rom mutant F14Yx-ray diffractionA, B, C——
2IJKStructure of a Rom protein dimer at 1.55 angstrom resolutionx-ray diffractionA, B——
2IJKStructure of a rom protein dimer at 1.55 ångström resolutionx-ray diffractionA, B——
3K79C38A, C52V Cysteine-Free Variant of Rop (Rom)x-ray diffractionA——
3K79C38A, C52V cysteine-free variant of rop (rom)x-ray diffractionA——
4DO2Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.x-ray diffractionA, B——
4DO2Crystal structure of the rop protein mutant D30P/A31G at resolution 1.4 resolution.x-ray diffractionA, B——
7KAERop protein variant with a buried tryptophanx-ray diffractionA, B——
P03051AlphaFold monomer V2.0 prediction for regulatory protein rop (P03051)———

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