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1AIP

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
C0003746molecular_functiontranslation elongation factor activity
C0005737cellular_componentcytoplasm
C0006412biological_processtranslation
C0006414biological_processtranslational elongation
D0003746molecular_functiontranslation elongation factor activity
D0005737cellular_componentcytoplasm
D0006412biological_processtranslation
D0006414biological_processtranslational elongation
E0003746molecular_functiontranslation elongation factor activity
E0003924molecular_functionGTPase activity
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0006412biological_processtranslation
E0006414biological_processtranslational elongation
F0003746molecular_functiontranslation elongation factor activity
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
F0005737cellular_componentcytoplasm
F0006412biological_processtranslation
F0006414biological_processtranslational elongation
G0003746molecular_functiontranslation elongation factor activity
G0005737cellular_componentcytoplasm
G0006412biological_processtranslation
G0006414biological_processtranslational elongation
H0003746molecular_functiontranslation elongation factor activity
H0005737cellular_componentcytoplasm
H0006412biological_processtranslation
H0006414biological_processtranslational elongation
Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DKapeERaRGITIntA
ChainResidueDetails
AASP51-ALA66

site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LReaTGaGMmDvKRAL
ChainResidueDetails
CLEU10-LEU25

site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. ELNCETDFVAR
ChainResidueDetails
CGLU75-ARG85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AHIS19
FHIS19
FCYS82
FLYS137
ACYS82
ALYS137
BHIS19
BCYS82
BLYS137
EHIS19
ECYS82
ELYS137

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250
ChainResidueDetails
AVAL395
BVAL395
EVAL395
FVAL395

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AASP21

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BASP21

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
EASP21

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
FASP21

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS85

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BHIS85

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
EHIS85

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
FHIS85

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PDB entries from 2024-07-17

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