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1XB2

Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016787molecular_functionhydrolase activity
A0032543biological_processmitochondrial translation
A0046872molecular_functionmetal ion binding
A0070125biological_processmitochondrial translational elongation
B0003746molecular_functiontranslation elongation factor activity
B0006414biological_processtranslational elongation
Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeERaRGITInaA
ChainResidueDetails
AASP96-ALA111

site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LRrkTGySFiNcKKAL
ChainResidueDetails
BLEU66-LEU81

site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. EVNCETDFVSR
ChainResidueDetails
BGLU133-ARG143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsRegion: {"description":"G3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0CE47","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P49411","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BFR5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P49411","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BFR5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BFR5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZR8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P43897","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AASP67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS130

246031

PDB entries from 2025-12-10

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