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UniProt P00648

Ribonuclease (P00648)

Ribonuclease (UniProt P00648), EC 3.1.27.-: 104 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound, 10 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P00648
Protein
Ribonuclease
EC
3.1.27.-
Experimental structures
104
Predicted models
1
Ligands
1
Pockets
10 · 2 records with a druggable one

Structures

105 records of P00648 in the MolNFT archive: 104 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1A2PBarnase wildtype structure at 1.5 ångströms resolutionx-ray diffractionA, B, C——
1A2PBarnase wildtype structure at 1.5 ångströms resolutionx-ray diffractionA, B, C——
1B20Deletion of a buried salt-bridge in barnasex-ray diffractionA, B, C——
1B20Deletion of a buried salt-bridge in barnasex-ray diffractionA, B, C——
1B21Deletion of a buried salt bridge in barnasex-ray diffractionA, B, C——
1B21Deletion of a buried salt bridge in barnasex-ray diffractionA, B, C——
1B27Structural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B27Structural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B2SStructural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B2SStructural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B2UStructural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B2UStructural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B2XBarnase wildtype structure at pH 7.5 from a CRYO_COOLED crystal at 100Kx-ray diffractionA, B, C——
1B2XBarnase wildtype structure at pH 7.5 from a CRYO_COOLED crystal at 100Kx-ray diffractionA, B, C——
1B2ZDeletion of a buried salt bridge in barnasex-ray diffractionA, B, C——
1B2ZDeletion of a buried salt bridge in barnasex-ray diffractionA, B, C——
1B3SStructural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1B3SStructural response to mutation at a protein-protein interfacex-ray diffractionA, B, C——
1BANThe contribution of buried hydrogen bonds to protein stability: the crystal structures of two…x-ray diffractionA, B, C——
1BANThe contribution of buried hydrogen bonds to protein stability: the crystal structures of two…x-ray diffractionA, B, C——
1BAOThe contribution of buried hydrogen bonds to protein stability: the crystal structures of two…x-ray diffractionA, B, C——
1BAOThe contribution of buried hydrogen bonds to protein stability: the crystal structures of two…x-ray diffractionA, B, C——
1BGSRecognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstarx-ray diffractionA, B, C——
1BGSRecognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstarx-ray diffractionA, B, C——
1BNEBarnase A43C/S80C disulfide mutantx-ray diffractionA, B, C——
1BNEBarnase A43C/S80C disulfide mutantx-ray diffractionA, B, C——
1BNFBarnase T70C/S92C disulfide mutantx-ray diffractionA, B, C——
1BNFBarnase T70C/S92C disulfide mutantx-ray diffractionA, B, C——
1BNGBarnase S85C/H102C disulfide mutantx-ray diffractionA, B, C——
1BNGBarnase S85C/H102C disulfide mutantx-ray diffractionA, B, C——
1BNIBarnase wildtype structure at pH 6.0x-ray diffractionA, B, C——
1BNIBarnase wildtype structure at pH 6.0x-ray diffractionA, B, C——
1BNJBarnase wildtype structure at pH 9.0x-ray diffractionA, B, C——
1BNJBarnase wildtype structure at pH 9.0x-ray diffractionA, B, C——
1BNRBARNASEsolution nmrA——
1BNRBARNASEsolution nmrA——
1BNSStructural studies of barnase mutantsx-ray diffractionA, B, C——
1BNSStructural studies of barnase mutantsx-ray diffractionA, B, C——
1BRGCrystallographic analysis of phe->leu substitution in the hydrophobic core of barnasex-ray diffractionA, B, C——
1BRGCrystallographic analysis of phe->leu substitution in the hydrophobic core of barnasex-ray diffractionA, B, C——
1BRHBarnase mutant with leu 14 replaced by alax-ray diffractionA, B, C——
1BRHBarnase mutant with leu 14 replaced by alax-ray diffractionA, B, C——
1BRIBarnase mutant with ile 76 replaced by alax-ray diffractionA, B, C——
1BRIBarnase mutant with ile 76 replaced by alax-ray diffractionA, B, C——
1BRJBarnase mutant with ile 88 replaced by alax-ray diffractionA, B, C——
1BRJBarnase mutant with ile 88 replaced by alax-ray diffractionA, B, C——
1BRKBarnase mutant with ile 96 replaced by alax-ray diffractionA, B, C——
1BRKBarnase mutant with ile 96 replaced by alax-ray diffractionA, B, C——
1BRNSubsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76 ångströms…x-ray diffractionL, M——
1BRNSubsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76 ångströms…x-ray diffractionL, M——
1BRSProtein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-a…x-ray diffractionA, B, C——
1BRSProtein-protein recognition: crystal structural analysis of a barnase- barstar complex at 2.0-a…x-ray diffractionA, B, C——
1BSACrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSACrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSBCrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSBCrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSCCrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSCCrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSDCrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——
1BSDCrystal structural analysis of mutations in the hydrophobic cores of barnasex-ray diffractionA, B, C——

45 records more on the page itself.

Ligands

  • PO4 · Phosphate ion · in 2 records

Experiment against prediction

Elsewhere

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