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P0A7R9

- RS11_ECOLI

UniProt

P0A7R9 - RS11_ECOLI

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Protein

30S ribosomal protein S11

Gene
rpsK, b3297, JW3259
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome By similarity.UniRule annotation

GO - Molecular functioni

  1. small ribosomal subunit rRNA binding Source: EcoliWiki
  2. structural constituent of ribosome Source: EcoliWiki

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10910-MONOMER.
ECOL316407:JW3259-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S11
Gene namesi
Name:rpsK
Ordered Locus Names:b3297, JW3259
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10910. rpsK.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12912830S ribosomal protein S11UniRule annotationPRO_0000123144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-methylalanineUniRule annotation

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP0A7R9.
PRIDEiP0A7R9.

Expressioni

Gene expression databases

GenevestigatoriP0A7R9.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18 By similarity. Cross-links to IF-3.1 Publication

Protein-protein interaction databases

BioGridi852104. 1 interaction.
DIPiDIP-47838N.
IntActiP0A7R9. 14 interactions.
MINTiMINT-1232137.
STRINGi511145.b3297.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 259
Beta strandi27 – 293
Beta strandi30 – 367
Turni37 – 393
Beta strandi43 – 475
Helixi48 – 503
Beta strandi54 – 563
Beta strandi57 – 593
Helixi60 – 7112
Turni72 – 743
Helixi75 – 773
Beta strandi79 – 9012
Helixi93 – 1019
Turni102 – 1043
Beta strandi106 – 1127

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-K13-129[»]
1P6Gelectron microscopy12.30K2-129[»]
1P87electron microscopy11.50K2-129[»]
1VS5X-ray3.46K1-129[»]
1VS7X-ray3.46K1-129[»]
2AVYX-ray3.46K2-129[»]
2AW7X-ray3.46K2-129[»]
2GY9electron microscopy15.00K13-128[»]
2GYBelectron microscopy15.00K13-128[»]
2I2PX-ray3.22K2-129[»]
2I2UX-ray3.22K2-129[»]
2QALX-ray3.21K2-129[»]
2QANX-ray3.21K2-129[»]
2QB9X-ray3.54K2-129[»]
2QBBX-ray3.54K2-129[»]
2QBDX-ray3.30K2-129[»]
2QBFX-ray3.30K2-129[»]
2QBHX-ray4.00K2-129[»]
2QBJX-ray4.00K2-129[»]
2QOUX-ray3.93K2-129[»]
2QOWX-ray3.93K2-129[»]
2QOYX-ray3.50K2-129[»]
2QP0X-ray3.50K2-129[»]
2VHOX-ray3.74K2-129[»]
2VHPX-ray3.74K2-129[»]
2WWLelectron microscopy5.80K13-129[»]
2YKRelectron microscopy9.80K13-129[»]
2Z4KX-ray4.45K2-129[»]
2Z4MX-ray4.45K2-129[»]
3DF1X-ray3.50K2-128[»]
3DF3X-ray3.50K2-129[»]
3E1Aelectron microscopy-C1-129[»]
3E1Celectron microscopy-C1-129[»]
3FIHelectron microscopy6.70K13-129[»]
3I1MX-ray3.19K1-129[»]
3I1OX-ray3.19K1-129[»]
3I1QX-ray3.81K1-129[»]
3I1SX-ray3.81K1-129[»]
3I1ZX-ray3.71K1-129[»]
3I21X-ray3.71K1-129[»]
3IZVelectron microscopy-O1-129[»]
3IZWelectron microscopy-O1-129[»]
3J00electron microscopy-K2-129[»]
3J0Uelectron microscopy12.10N2-129[»]
3J0Velectron microscopy14.70N2-129[»]
3J0Xelectron microscopy13.50N2-129[»]
3J0Zelectron microscopy11.50N2-129[»]
3J10electron microscopy11.50N2-129[»]
3J13electron microscopy13.10M2-129[»]
3J18electron microscopy8.30K13-129[»]
3J36electron microscopy9.80K2-129[»]
3J4Velectron microscopy12.00K13-129[»]
3J4Welectron microscopy12.00K13-129[»]
3J4Yelectron microscopy17.00K13-129[»]
3J4Zelectron microscopy20.00K13-129[»]
3J53electron microscopy13.00K13-129[»]
3J55electron microscopy15.00K13-129[»]
3J57electron microscopy17.00K13-129[»]
3J59electron microscopy12.00K13-129[»]
3J5Belectron microscopy17.00K13-129[»]
3J5Delectron microscopy17.00K13-129[»]
3J5Felectron microscopy20.00K13-129[»]
3J5Helectron microscopy15.00K13-129[»]
3J5Jelectron microscopy9.00K13-129[»]
3J5Nelectron microscopy6.80K1-129[»]
3J5Telectron microscopy7.60K2-129[»]
3J5Xelectron microscopy7.60K2-129[»]
3KC4electron microscopy-K1-129[»]
3OAQX-ray3.25K13-129[»]
3OARX-ray3.25K13-129[»]
3OFAX-ray3.19K13-129[»]
3OFBX-ray3.19K13-129[»]
3OFOX-ray3.10K13-129[»]
3OFPX-ray3.10K13-129[»]
3OFXX-ray3.29K13-129[»]
3OFYX-ray3.29K13-129[»]
3OR9X-ray3.30K1-129[»]
3ORAX-ray3.30K1-129[»]
3SFSX-ray3.20K1-129[»]
3UOQX-ray3.70K1-129[»]
4A2Ielectron microscopy16.50K13-129[»]
4ADVelectron microscopy13.50K2-129[»]
4GAQX-ray3.30K1-129[»]
4GASX-ray3.30K1-129[»]
4GD1X-ray3.00K13-129[»]
4GD2X-ray3.00K13-129[»]
4KIYX-ray2.90K1-129[»]
4KJ0X-ray2.90K1-129[»]
4KJ2X-ray2.90K1-129[»]
4KJ4X-ray2.90K1-129[»]
4KJ6X-ray2.90K1-129[»]
4KJ8X-ray2.90K1-129[»]
4KJAX-ray2.90K1-129[»]
4KJCX-ray2.90K1-129[»]
ProteinModelPortaliP0A7R9.
SMRiP0A7R9. Positions 2-129.

Miscellaneous databases

EvolutionaryTraceiP0A7R9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0100.
HOGENOMiHOG000111598.
KOiK02948.
OMAiHISASFN.
OrthoDBiEOG6ZSPF3.
PhylomeDBiP0A7R9.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsiTIGR03632. bact_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7R9-1 [UniParc]FASTAAdd to Basket

« Hide

MAKAPIRARK RVRKQVSDGV AHIHASFNNT IVTITDRQGN ALGWATAGGS    50
GFRGSRKSTP FAAQVAAERC ADAVKEYGIK NLEVMVKGPG PGRESTIRAL 100
NAAGFRITNI TDVTPIPHNG CRPPKKRRV 129
Length:129
Mass (Da):13,845
Last modified:January 23, 2007 - v2
Checksum:i0C759DDA60E89C0C
GO

Mass spectrometryi

Molecular mass is 13727.7 Da from positions 2 - 129. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02543 Genomic DNA. Translation: CAA26393.1.
U18997 Genomic DNA. Translation: AAA58095.1.
U00096 Genomic DNA. Translation: AAC76322.1.
AP009048 Genomic DNA. Translation: BAE77994.1.
PIRiB23807. R3EC11.
RefSeqiNP_417756.1. NC_000913.3.
YP_492135.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76322; AAC76322; b3297.
BAE77994; BAE77994; BAE77994.
GeneIDi12934439.
947792.
KEGGiecj:Y75_p3879.
eco:b3297.
PATRICi32122026. VBIEscCol129921_3390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02543 Genomic DNA. Translation: CAA26393.1 .
U18997 Genomic DNA. Translation: AAA58095.1 .
U00096 Genomic DNA. Translation: AAC76322.1 .
AP009048 Genomic DNA. Translation: BAE77994.1 .
PIRi B23807. R3EC11.
RefSeqi NP_417756.1. NC_000913.3.
YP_492135.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5G model - K 13-129 [» ]
1P6G electron microscopy 12.30 K 2-129 [» ]
1P87 electron microscopy 11.50 K 2-129 [» ]
1VS5 X-ray 3.46 K 1-129 [» ]
1VS7 X-ray 3.46 K 1-129 [» ]
2AVY X-ray 3.46 K 2-129 [» ]
2AW7 X-ray 3.46 K 2-129 [» ]
2GY9 electron microscopy 15.00 K 13-128 [» ]
2GYB electron microscopy 15.00 K 13-128 [» ]
2I2P X-ray 3.22 K 2-129 [» ]
2I2U X-ray 3.22 K 2-129 [» ]
2QAL X-ray 3.21 K 2-129 [» ]
2QAN X-ray 3.21 K 2-129 [» ]
2QB9 X-ray 3.54 K 2-129 [» ]
2QBB X-ray 3.54 K 2-129 [» ]
2QBD X-ray 3.30 K 2-129 [» ]
2QBF X-ray 3.30 K 2-129 [» ]
2QBH X-ray 4.00 K 2-129 [» ]
2QBJ X-ray 4.00 K 2-129 [» ]
2QOU X-ray 3.93 K 2-129 [» ]
2QOW X-ray 3.93 K 2-129 [» ]
2QOY X-ray 3.50 K 2-129 [» ]
2QP0 X-ray 3.50 K 2-129 [» ]
2VHO X-ray 3.74 K 2-129 [» ]
2VHP X-ray 3.74 K 2-129 [» ]
2WWL electron microscopy 5.80 K 13-129 [» ]
2YKR electron microscopy 9.80 K 13-129 [» ]
2Z4K X-ray 4.45 K 2-129 [» ]
2Z4M X-ray 4.45 K 2-129 [» ]
3DF1 X-ray 3.50 K 2-128 [» ]
3DF3 X-ray 3.50 K 2-129 [» ]
3E1A electron microscopy - C 1-129 [» ]
3E1C electron microscopy - C 1-129 [» ]
3FIH electron microscopy 6.70 K 13-129 [» ]
3I1M X-ray 3.19 K 1-129 [» ]
3I1O X-ray 3.19 K 1-129 [» ]
3I1Q X-ray 3.81 K 1-129 [» ]
3I1S X-ray 3.81 K 1-129 [» ]
3I1Z X-ray 3.71 K 1-129 [» ]
3I21 X-ray 3.71 K 1-129 [» ]
3IZV electron microscopy - O 1-129 [» ]
3IZW electron microscopy - O 1-129 [» ]
3J00 electron microscopy - K 2-129 [» ]
3J0U electron microscopy 12.10 N 2-129 [» ]
3J0V electron microscopy 14.70 N 2-129 [» ]
3J0X electron microscopy 13.50 N 2-129 [» ]
3J0Z electron microscopy 11.50 N 2-129 [» ]
3J10 electron microscopy 11.50 N 2-129 [» ]
3J13 electron microscopy 13.10 M 2-129 [» ]
3J18 electron microscopy 8.30 K 13-129 [» ]
3J36 electron microscopy 9.80 K 2-129 [» ]
3J4V electron microscopy 12.00 K 13-129 [» ]
3J4W electron microscopy 12.00 K 13-129 [» ]
3J4Y electron microscopy 17.00 K 13-129 [» ]
3J4Z electron microscopy 20.00 K 13-129 [» ]
3J53 electron microscopy 13.00 K 13-129 [» ]
3J55 electron microscopy 15.00 K 13-129 [» ]
3J57 electron microscopy 17.00 K 13-129 [» ]
3J59 electron microscopy 12.00 K 13-129 [» ]
3J5B electron microscopy 17.00 K 13-129 [» ]
3J5D electron microscopy 17.00 K 13-129 [» ]
3J5F electron microscopy 20.00 K 13-129 [» ]
3J5H electron microscopy 15.00 K 13-129 [» ]
3J5J electron microscopy 9.00 K 13-129 [» ]
3J5N electron microscopy 6.80 K 1-129 [» ]
3J5T electron microscopy 7.60 K 2-129 [» ]
3J5X electron microscopy 7.60 K 2-129 [» ]
3KC4 electron microscopy - K 1-129 [» ]
3OAQ X-ray 3.25 K 13-129 [» ]
3OAR X-ray 3.25 K 13-129 [» ]
3OFA X-ray 3.19 K 13-129 [» ]
3OFB X-ray 3.19 K 13-129 [» ]
3OFO X-ray 3.10 K 13-129 [» ]
3OFP X-ray 3.10 K 13-129 [» ]
3OFX X-ray 3.29 K 13-129 [» ]
3OFY X-ray 3.29 K 13-129 [» ]
3OR9 X-ray 3.30 K 1-129 [» ]
3ORA X-ray 3.30 K 1-129 [» ]
3SFS X-ray 3.20 K 1-129 [» ]
3UOQ X-ray 3.70 K 1-129 [» ]
4A2I electron microscopy 16.50 K 13-129 [» ]
4ADV electron microscopy 13.50 K 2-129 [» ]
4GAQ X-ray 3.30 K 1-129 [» ]
4GAS X-ray 3.30 K 1-129 [» ]
4GD1 X-ray 3.00 K 13-129 [» ]
4GD2 X-ray 3.00 K 13-129 [» ]
4KIY X-ray 2.90 K 1-129 [» ]
4KJ0 X-ray 2.90 K 1-129 [» ]
4KJ2 X-ray 2.90 K 1-129 [» ]
4KJ4 X-ray 2.90 K 1-129 [» ]
4KJ6 X-ray 2.90 K 1-129 [» ]
4KJ8 X-ray 2.90 K 1-129 [» ]
4KJA X-ray 2.90 K 1-129 [» ]
4KJC X-ray 2.90 K 1-129 [» ]
ProteinModelPortali P0A7R9.
SMRi P0A7R9. Positions 2-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852104. 1 interaction.
DIPi DIP-47838N.
IntActi P0A7R9. 14 interactions.
MINTi MINT-1232137.
STRINGi 511145.b3297.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7R9.
PRIDEi P0A7R9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76322 ; AAC76322 ; b3297 .
BAE77994 ; BAE77994 ; BAE77994 .
GeneIDi 12934439.
947792.
KEGGi ecj:Y75_p3879.
eco:b3297.
PATRICi 32122026. VBIEscCol129921_3390.

Organism-specific databases

EchoBASEi EB0903.
EcoGenei EG10910. rpsK.

Phylogenomic databases

eggNOGi COG0100.
HOGENOMi HOG000111598.
KOi K02948.
OMAi HISASFN.
OrthoDBi EOG6ZSPF3.
PhylomeDBi P0A7R9.

Enzyme and pathway databases

BioCyci EcoCyc:EG10910-MONOMER.
ECOL316407:JW3259-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7R9.
PROi P0A7R9.

Gene expression databases

Genevestigatori P0A7R9.

Family and domain databases

Gene3Di 3.30.420.80. 1 hit.
HAMAPi MF_01310. Ribosomal_S11.
InterProi IPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view ]
PANTHERi PTHR11759. PTHR11759. 1 hit.
Pfami PF00411. Ribosomal_S11. 1 hit.
[Graphical view ]
PIRSFi PIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsi TIGR03632. bact_S11. 1 hit.
PROSITEi PS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli."
    Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L.
    Nucleic Acids Res. 13:3891-3903(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Primary structure of protein S11 from Escherichia coli ribosomes."
    Kamp R., Wittmann-Liebold B.
    FEBS Lett. 121:117-122(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-129.
    Strain: K.
  5. "Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits."
    MacKeen L.A., Kahan L., Wahba A.J., Schwartz I.
    J. Biol. Chem. 255:10526-10531(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO IF-3.
    Strain: B.
  6. "IF-3 crosslinking to Escherichia coli ribosomal 30 S subunits by three different light-dependent procedures: identification of 30 S proteins crosslinked to IF-3 -- utilization of a new two-stage crosslinking reagent, p-nitrobenzylmaleimide."
    Cooperman B.S., Expert-Bezancon A., Kahan L., Dondon J., Grunberg-Manago M.
    Arch. Biochem. Biophys. 208:554-562(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO IF-3.
  7. "Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane."
    Boileau G., Butler P., Hershey J.W.B., Traut R.R.
    Biochemistry 22:3162-3170(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO IF-3.
    Strain: MRE-600.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  10. "Interaction of translation initiation factor 3 with the 30S ribosomal subunit."
    Dallas A., Noller H.F.
    Mol. Cell 8:855-864(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MODELING OF IF-3/30S SUBUNIT INTERACTION.
  11. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  12. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS11_ECOLI
AccessioniPrimary (citable) accession number: P0A7R9
Secondary accession number(s): P02366, Q2M6W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies (1 Publication); exactly how IF-3 interacts with the 30S subunit is controversial.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi