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4PC7

Elongation factor Tu:Ts complex in a near GTP conformation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0097216molecular_functionguanosine tetraphosphate binding
C0003746molecular_functiontranslation elongation factor activity
C0005085molecular_functionguanyl-nucleotide exchange factor activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006414biological_processtranslational elongation
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
C0032045cellular_componentguanyl-nucleotide exchange factor complex
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GNP A 401
ChainResidue
AVAL20
AASN135
ALYS136
AASP138
AMET139
ASER173
AALA174
ALEU175
AMG403
AHOH501
AASP21
AHIS22
AGLY23
ALYS24
ATHR25
ATHR26
APRO82
AGLY83

site_idAC2
Number of Residues21
Detailsbinding site for residue PUL A 402
ChainResidue
AILE92
ATHR93
AGLN97
AGLN124
AVAL125
APRO213
AGLU215
ATHR228
AGLY229
AARG230
AGLU259
APHE261
AARG262
AASN273
AVAL274
ATYR331
AARG333
ATHR334
AARG373
AALA375
AARG377

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
ATHR25
AASP80
ACYS81
AGNP401
AHOH501

Functional Information from PROSITE/UniProt
site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL
ChainResidueDetails
CLEU11-LEU26

site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK
ChainResidueDetails
CGLU74-LYS84

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 Residues4
DetailsM-CSA 535
ChainResidueDetails
AASP21electrostatic stabiliser
ALYS24electrostatic stabiliser
ATHR25metal ligand
AHIS84electrostatic stabiliser

219869

PDB entries from 2024-05-15

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