#IFEStandardized nameMoleculeOrganismSourceRfamTitleMethodRes. ÅDate
11EHZ|A (rep)Transfer RNASaccharomyces cerevisiaeEukaryaRF00005The crystal structure of yeast phenylalanine tRNA at 1.93 A resolutionX-ray diffraction1.932000-10-02
21EVV|ATransfer RNASaccharomycesEukaryaRF00005CRYSTAL STRUCTURE OF YEAST PHENYLALANINE TRANSFER RNA AT 2.0 A RESOLUTIONX-ray diffraction22000-05-01
31FCW|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11
41I9V|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEXX-ray diffraction2.62001-06-04
51MJ1|CTransfer RNAEscherichia coliBacteriaRF00005FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GTP AND RIBOSOMAL PROTEINS INTO A 13 A CRYO-EM MAP OF THE COLI 70S RIBOSOMEElectron microscopy132002-11-01
61ML5|aLarge subunit ribosomal RNAEscherichia coliBacteriaRF02541Structure of the E. coli ribosomal termination complex with release factor 2Electron microscopy142003-01-14
71OB2|BTransfer RNASaccharomyces cerevisiaeEukaryaRF00005E. coli elongation factor EF-Tu complexed with the antibiotic kirromycin, a GTP analog, and Phe-tRNAX-ray diffraction3.352004-05-27
81OB5|BTransfer RNASaccharomyces cerevisiaeEukaryaRF00005T. aquaticus elongation factor EF-Tu complexed with the antibiotic enacyloxin IIa, a GTP analog, and Phe-tRNAX-ray diffraction3.12005-10-13
91SZ1|EMechanism of CCA-adding enzymes specificity revealed by crystal structures of ternary complexesX-ray diffraction6.212004-08-10
101TN1|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE TRNAX-ray diffraction31987-01-15
111TN2|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE T-RNAX-ray diffraction31986-10-24
121TRA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005RESTRAINED REFINEMENT OF THE MONOCLINIC FORM OF YEAST PHENYLALANINE TRANSFER RNA. TEMPERATURE FACTORS AND DYNAMICS, COORDINATED WATERS, AND BASE-PAIR PROPELLER TWIST ANGLESX-ray diffraction31986-07-14
131TTT|DPhe-tRNA, elongation factoR EF-TU:GDPNP ternary complexX-ray diffraction2.71996-12-23
141ZO1|FTransfer RNAEscherichia coliBacteriaRF00005IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complexElectron microscopy13.82005-06-14
151ZO3|ATransfer RNAEscherichia coliBacteriaRF00005The P-site and P/E-site tRNA structures fitted to P/I site codon.Electron microscopy13.82005-06-14
163IZY|NTransfer RNABos taurusMitochondriaRF00005Mammalian mitochondrial translation initiation factor 2Electron microscopy10.82011-03-23
173WC2|PCrystal structure of C. albicans tRNA(His) guanylyltransferase (Thg1) with a tRNA(Phe)(GUG)X-ray diffraction3.642013-12-18
184TNA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005FURTHER REFINEMENT OF THE STRUCTURE OF YEAST T-RNA-PHEX-ray diffraction2.51978-04-12
194TRA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005RESTRAINED REFINEMENT OF TWO CRYSTALLINE FORMS OF YEAST ASPARTIC ACID AND PHENYLALANINE TRANSFER RNA CRYSTALSX-ray diffraction31987-11-06
206TNA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTAL STRUCTURE OF YEAST PHENYLALANINE T-RNA. I.CRYSTALLOGRAPHIC REFINEMENTX-ray diffraction2.71979-01-16

Release history

Release1.411.421.431.441.451.461.471.481.491.501.511.521.531.541.551.561.571.581.591.601.611.621.631.641.651.661.671.681.691.701.711.721.731.741.751.761.771.781.791.801.811.821.831.841.851.861.871.881.89
Date2013-12-212013-12-282014-01-042014-01-112014-01-182014-01-252014-02-012014-02-082014-02-152014-02-222014-03-012014-03-082014-03-172014-03-222014-03-292014-04-052014-04-122014-04-192014-04-262014-05-032014-05-102014-05-172014-05-312014-06-072014-06-132014-06-202014-06-272014-07-042014-07-182014-07-252014-08-012014-08-082014-08-152014-08-222014-08-292014-09-052014-09-122014-09-192014-09-262014-10-032014-10-102014-10-172014-10-242014-10-312014-11-072014-11-142014-11-212014-11-282014-12-05

Parents

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Children

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Instances are ordered to put similar structures near each other. Select one instance to see its 3D structure. Selecting two or more instances will show their superposition, but only chains with identical numbers of observed nucleotides will superpose well. Large structures are slow to display; this tool is not designed for that.

#SViewPDBTitleMethodResolutionLength

Heat map of mutual geometric discrepancy, in Angstroms per nucleotide. The ordering in the heat map is the same as in the table. The colorbar ranges from 0 to the maximum observed discrepancy. Click above the diagonal to select a range of structures, below the diagonal to select two structures.


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