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1EGA

CRYSTAL STRUCTURE OF A WIDELY CONSERVED GTPASE ERA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000028biological_processribosomal small subunit assembly
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0009898cellular_componentcytoplasmic side of plasma membrane
A0019843molecular_functionrRNA binding
A0042254biological_processribosome biogenesis
A0042274biological_processribosomal small subunit biogenesis
A0043024molecular_functionribosomal small subunit binding
A0046777biological_processprotein autophosphorylation
A0070181molecular_functionsmall ribosomal subunit rRNA binding
A0097216molecular_functionguanosine tetraphosphate binding
B0000028biological_processribosomal small subunit assembly
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0009898cellular_componentcytoplasmic side of plasma membrane
B0019843molecular_functionrRNA binding
B0042254biological_processribosome biogenesis
B0042274biological_processribosomal small subunit biogenesis
B0043024molecular_functionribosomal small subunit binding
B0046777biological_processprotein autophosphorylation
B0070181molecular_functionsmall ribosomal subunit rRNA binding
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AASN18
AVAL19
AGLY20
ALYS21
ASER22

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
ATHR23
AASN26
ALYS27
ATHR36
ATHR215
ALYS282

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BASN18
BVAL19
BGLY20
BLYS21
BSER22

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BTHR23
BASN26
BLYS27
BTHR36
BTHR215
BLYS282

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ALYS32
ATYR212
AHOH374
AHOH405

site_idHG
Number of Residues4
DetailsMERCURY ATOM-BINDING SITES IN EMP DERIVATIVE USED IN MAD PHASING
ChainResidue
ACYS8
AHIS51
BCYS8
BHIS51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues336
DetailsDomain: {"description":"Era-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues154
DetailsDomain: {"description":"KH type-2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsRegion: {"description":"G1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsRegion: {"description":"G2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsRegion: {"description":"G3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsRegion: {"description":"G4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsRegion: {"description":"G5","evidences":[{"source":"PROSITE-ProRule","id":"PRU01050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3097637","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"8057845","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
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
AASP62

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BASP62

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ALEU66

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BLEU66

247536

PDB entries from 2026-01-14

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