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5I4R

Contact-dependent inhibition system from Escherichia coli NC101 - ternary CdiA/CdiI/EF-Tu complex (trypsin-modified)

Functional Information from GO Data
ChainGOidnamespacecontents
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
D0003746molecular_functiontranslation elongation factor activity
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
D0006414biological_processtranslational elongation
G0003924molecular_functionGTPase activity
G0005525molecular_functionGTP binding
H0003746molecular_functiontranslation elongation factor activity
H0003924molecular_functionGTPase activity
H0005525molecular_functionGTP binding
H0006414biological_processtranslational elongation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue GDP C 101
ChainResidue
CASP22
DSER174
DALA175
DLEU176
CGLY24
CLYS25
CTHR26
CTHR27
DASN136
DLYS137
DASP139
DMET140

site_idAC2
Number of Residues13
Detailsbinding site for residue GDP G 101
ChainResidue
GASP22
GHIS23
GGLY24
GLYS25
GTHR26
GTHR27
HASN136
HLYS137
HASP139
HMET140
HSER174
HALA175
HLEU176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
DASP81
DASN136
HASP81
HASN136

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
DLYS314
HLYS314

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965
ChainResidueDetails
DTHR383
HTHR383

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 535
ChainResidueDetails
DHIS85electrostatic stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 535
ChainResidueDetails
HHIS85electrostatic stabiliser

225158

PDB entries from 2024-09-18

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