Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1X1L

Interaction of ERA,a GTPase protein, with the 3'minor domain of the 16S rRNA within the THERMUS THERMOPHILUS 30S subunit.

Functional Information from GO Data
ChainGOidnamespacecontents
X0000028biological_processribosomal small subunit assembly
X0000166molecular_functionnucleotide binding
X0003723molecular_functionRNA binding
X0003924molecular_functionGTPase activity
X0005515molecular_functionprotein binding
X0005525molecular_functionGTP binding
X0005737cellular_componentcytoplasm
X0005829cellular_componentcytosol
X0005886cellular_componentplasma membrane
X0006468biological_processprotein phosphorylation
X0009898cellular_componentcytoplasmic side of plasma membrane
X0019843molecular_functionrRNA binding
X0042254biological_processribosome biogenesis
X0042274biological_processribosomal small subunit biogenesis
X0043024molecular_functionribosomal small subunit binding
X0046777biological_processprotein autophosphorylation
X0070181molecular_functionsmall ribosomal subunit rRNA binding
X0097216molecular_functionguanosine tetraphosphate binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues168
DetailsDomain: {"description":"Era-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues77
DetailsDomain: {"description":"KH type-2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsRegion: {"description":"G2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsRegion: {"description":"G3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3097637","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"8057845","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"8057845","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
XASP62

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
XLEU66

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon