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5JBQ

EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH THIOMURACIN ANALOG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016020cellular_componentmembrane
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP A 401
ChainResidue
AASP21
AASP138
AMET139
ASER173
AALA174
ALEU175
AMG403
AHOH576
AHOH578
AHOH603
AHOH627
AHIS22
AHOH654
AGLY23
ALYS24
ATHR25
ATHR26
APHE46
AASN135
ALYS136

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH510
AHOH510
AHOH554
AHOH554
AHOH636
AHOH636

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
ATHR25
AGDP401

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AARG262
AARG318
AHIS319
ATHR320
AARG381

site_idAC5
Number of Residues27
DetailsBINDING SITE FOR CHAIN B OF THIOMURACIN ANALOG
ChainResidue
ATHR73
AALA182
AGLU215
AILE220
AARG223
ATHR228
AGLY257
AGLU259
APHE261
AARG262
ALEU264
AASN273
AVAL274
AGLY275
ALEU277
ATHR320
APRO321
APHE323
ALYS324
AGLY325
AHOH527
BHOH101
BHOH102
BHOH103
BHOH104
BHOH105
BHOH106

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS
ChainResidueDetails
AASP50-SER65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AGLY18
AASP80
AASN135

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ASER1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ALYS56

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS313

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965
ChainResidueDetails
ATHR382

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 535
ChainResidueDetails
AASP21electrostatic stabiliser
ALYS24electrostatic stabiliser
ATHR25metal ligand
AGLY83electrostatic stabiliser
AHIS84electrostatic stabiliser

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PDB entries from 2024-04-24

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