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4ZV4

Structure of Tse6 in complex with EF-Tu

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016787molecular_functionhydrolase activity
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0016787molecular_functionhydrolase activity
B0032045cellular_componentguanyl-nucleotide exchange factor complex
B0046872molecular_functionmetal ion binding
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue GDP A 501
ChainResidue
AASP22
AASP139
AMET140
ASER174
ALEU176
AMG502
AHIS23
AGLY24
ALYS25
ATHR26
ATHR27
APRO83
AASN136
ALYS137

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
ATHR26
AASP81
APRO83
AGDP501

site_idAC3
Number of Residues11
Detailsbinding site for residue GDP B 501
ChainResidue
BVAL21
BASP22
BHIS23
BGLY24
BLYS25
BTHR26
BTHR27
BPHE47
BLYS137
BLEU176
BMG502

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BTHR26
BASP81
BCYS82
BGDP501

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS
ChainResidueDetails
AASP51-SER66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118
ChainResidueDetails
AGLY19
ATHR26
AASP81
AASN136
BGLY19
BTHR26
BASP81
BASN136

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PDB entries from 2025-06-18

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