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7VMX

The Crystal Structure of EF-Tu and EF-Ts complex from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003746molecular_functiontranslation elongation factor activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0009274cellular_componentpeptidoglycan-based cell wall
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0001666biological_processresponse to hypoxia
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0009274cellular_componentpeptidoglycan-based cell wall
B0010039biological_processresponse to iron ion
B0016787molecular_functionhydrolase activity
B0035375molecular_functionzymogen binding
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeERqRGITIniA
ChainResidueDetails
BASP53-ALA68

site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LRelTGaGMlAcKNAL
ChainResidueDetails
ALEU12-LEU27

site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. ELNCETDFVAK
ChainResidueDetails
AGLU71-LYS81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118
ChainResidueDetails
BGLY19
BTHR26
BASP83
BASN138

238268

PDB entries from 2025-07-02

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