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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

10PX

Crystal structure of the wild-type Thermus thermophilus 70S ribosome in complex with benzoxaborole derivative of azithromycin (AZI-BB2), mRNA, aminoacylated A-site Phe-tRNAphe, aminoacylated P-site fMet-tRNAmet, and deacylated E-site tRNAphe at 2.45A resolution

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00049
Number of Residues27
DetailsRIBOSOMAL_L14 Ribosomal protein L14 signature. AVVVrtkkeikrp.DGsairFddNaaVI
ChainResidueDetails
1OALA60-ILE86
site_idPS00052
Number of Residues27
DetailsRIBOSOMAL_S7 Ribosomal protein S7 signature. DvLvtaFInkimrdGKKnlaarIFydA
ChainResidueDetails
1gASP20-ALA46
site_idPS00053
Number of Residues18
DetailsRIBOSOMAL_S8 Ribosomal protein S8 signature. GiaILSTSkGVLtdreAR
ChainResidueDetails
1hGLY108-ARG125
site_idPS00054
Number of Residues23
DetailsRIBOSOMAL_S11 Ribosomal protein S11 signature. IrALqaS.GLqVksivDdTPvPHN
ChainResidueDetails
1kILE95-ASN117
site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR
ChainResidueDetails
1lLYS46-ARG53
site_idPS00056
Number of Residues13
DetailsRIBOSOMAL_S17 Ribosomal protein S17 signature. GDvVeIiEsRPIS
ChainResidueDetails
1qGLY54-SER66
site_idPS00057
Number of Residues24
DetailsRIBOSOMAL_S18 Ribosomal protein S18 signature. RDYrn.VevLkrFLSEt.GKIlprRR
ChainResidueDetails
2rARG32-ARG55
site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LAKTIKraRIlGLlPF
ChainResidueDetails
2rLEU66-PHE81
site_idPS00196
Number of Residues16
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. GrvY.VICenPkHkqr.Q
ChainResidueDetails
19GLY21-GLN36
site_idPS00323
Number of Residues25
DetailsRIBOSOMAL_S19 Ribosomal protein S19 signature. NGKqhvpvyItenmVGhkLGEFapT
ChainResidueDetails
2sASN53-THR77
site_idPS00358
Number of Residues17
DetailsRIBOSOMAL_L5 Ribosomal protein L5 signature. LalITGQkpAvTrAKkS
ChainResidueDetails
1GLEU60-SER76
site_idPS00360
Number of Residues19
DetailsRIBOSOMAL_S9 Ribosomal protein S9 signature. GGGksGQidAiklGiARAL
ChainResidueDetails
1iGLY67-LEU85
site_idPS00361
Number of Residues16
DetailsRIBOSOMAL_S10 Ribosomal protein S10 signature. ArrsGAqvsGPIpLPT
ChainResidueDetails
1jALA27-THR42
site_idPS00362
Number of Residues31
DetailsRIBOSOMAL_S15 Ribosomal protein S15 signature. LseHLkvhKkDhhShrgLlmMvgqrrrLlrY
ChainResidueDetails
1oLEU39-TYR69
site_idPS00464
Number of Residues25
DetailsRIBOSOMAL_L22 Ribosomal protein L22 signature. KrvLpRArGRadiikkrtSHITViL
ChainResidueDetails
1WLYS83-LEU107
site_idPS00467
Number of Residues12
DetailsRIBOSOMAL_L2 Ribosomal protein L2 signature. PhvRGAAmNPvD
ChainResidueDetails
1DPRO219-ASP230
site_idPS00474
Number of Residues24
DetailsRIBOSOMAL_L3 Ribosomal protein L3 signature. FkpgervDvtGtSkGRGfaGvmkR
ChainResidueDetails
1EPHE96-ARG119
site_idPS00475
Number of Residues30
DetailsRIBOSOMAL_L15 Ribosomal protein L15 signature. KILGeGeAkp...LkVvahaFSksAlekLkaaG
ChainResidueDetails
1PLYS113-GLY142
site_idPS00527
Number of Residues23
DetailsRIBOSOMAL_S14 Ribosomal protein S14 signature. R.CvrcgrarsvyrfFGLCRiCLR
ChainResidueDetails
1nARG23-ARG45
site_idPS00548
Number of Residues35
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. ARtewaaqGrVplHt..LranIDygfalarTtyGvlG
ChainResidueDetails
1cALA163-GLY197
site_idPS00579
Number of Residues15
DetailsRIBOSOMAL_L29 Ribosomal protein L29 signature. QNHKIRdLKRQIARL
ChainResidueDetails
22GLN46-LEU60
site_idPS00582
Number of Residues20
DetailsRIBOSOMAL_L33 Ribosomal protein L33 signature. YaTeKNkrntPnkLElrKYC
ChainResidueDetails
16TYR21-CYS40
site_idPS00585
Number of Residues33
DetailsRIBOSOMAL_S5 Ribosomal protein S5 signature. GRrfrFgAlvVVGDrq.GrVGlGfgkap.EVpl.AV
ChainResidueDetails
1eGLY23-VAL55
site_idPS00632
Number of Residues25
DetailsRIBOSOMAL_S4 Ribosomal protein S4 signature. LEsRLdnvVYRlgfAvSrrqARqLV
ChainResidueDetails
1dLEU97-VAL121
site_idPS00634
Number of Residues33
DetailsRIBOSOMAL_L30 Ribosomal protein L30 signature. ALkaLgLrRlqQeRvledtpairgNVekVahLV
ChainResidueDetails
23ALA22-VAL54
site_idPS00646
Number of Residues14
DetailsRIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGlRHrrGlpVRGQ
ChainResidueDetails
1mARG88-GLN101
site_idPS00651
Number of Residues28
DetailsRIBOSOMAL_L9 Ribosomal protein L9 signature. GdvGqvvdVkpGYarNYLlprglAvlaT
ChainResidueDetails
1IGLY13-THR40
site_idPS00783
Number of Residues23
DetailsRIBOSOMAL_L13 Ribosomal protein L13 signature. VKGMLPkgpl.GRrlfkrLkVYaG
ChainResidueDetails
1NVAL103-GLY125
site_idPS00784
Number of Residues20
DetailsRIBOSOMAL_L34 Ribosomal protein L34 signature. KRTWQpnrrkRakth.GFraR
ChainResidueDetails
17LYS2-ARG21
site_idPS00828
Number of Residues26
DetailsRIBOSOMAL_L36 Ribosomal protein L36 signature. CdkCkvIrRhgrVyViCenp.KHkQrQ
ChainResidueDetails
19CYS11-GLN36
site_idPS00831
Number of Residues15
DetailsRIBOSOMAL_L27 Ribosomal protein L27 signature. GnILvRQRGtrfkpG
ChainResidueDetails
10GLY34-GLY48
site_idPS00936
Number of Residues27
DetailsRIBOSOMAL_L35 Ribosomal protein L35 signature. KTHkGAkKRVkitasgkvvamktgk.RH
ChainResidueDetails
18LYS5-HIS31
site_idPS00937
Number of Residues17
DetailsRIBOSOMAL_L20 Ribosomal protein L20 signature. KrdfRrLWIVRINaacR
ChainResidueDetails
1ULYS54-ARG70
site_idPS00962
Number of Residues12
DetailsRIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VkELLEAGVHFG
ChainResidueDetails
1bVAL7-GLY18
site_idPS01015
Number of Residues16
DetailsRIBOSOMAL_L19 Ribosomal protein L19 signature. IvQrGRAR.RAKLYFIR
ChainResidueDetails
1TILE88-ARG103
site_idPS01048
Number of Residues10
DetailsRIBOSOMAL_S6 Ribosomal protein S6 signature. GlRRLAYpIA
ChainResidueDetails
1fGLY44-ALA53
site_idPS01108
Number of Residues18
DetailsRIBOSOMAL_L24 Ribosomal protein L24 signature. GDtVlVAsGkyKGrv.GkV
ChainResidueDetails
1YGLY10-VAL27
site_idPS01143
Number of Residues22
DetailsRIBOSOMAL_L31 Ribosomal protein L31 signature. EVcskcHPFYTgqqrfvdte....GR
ChainResidueDetails
24GLU34-ARG55
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues224
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues38
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues56
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00501","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P80256","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues90
DetailsCoiled coil: {}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues136
DetailsDomain: {"description":"KH type-2"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues124
DetailsDomain: {"description":"S4 RNA-binding"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11866529","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues126
DetailsDomain: {"description":"S5 DRBM"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"3-methylthioaspartic acid","evidences":[{"source":"PubMed","id":"16287167","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25775268","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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