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1EFC

INTACT ELONGATION FACTOR FROM E.COLI

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
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0016020cellular_componentmembrane
B0032045cellular_componentguanyl-nucleotide exchange factor complex
B0046677biological_processresponse to antibiotic
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ATHR25
AGDP513
AHOH514
AHOH518
AHOH523
AHOH525

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BHOH521
BHOH522
BHOH523
BTHR25
BGDP514
BHOH520

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP A 513
ChainResidue
AASP21
AHIS22
AGLY23
ALYS24
ATHR25
ATHR26
APHE46
AASN135
ALYS136
AASP138
AMET139
ASER173
AALA174
ALEU175
AMG501
AHOH518
AHOH523
AHOH551
AHOH613
AHOH621
AHOH643
AHOH698
AHOH717

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP B 514
ChainResidue
BASP21
BHIS22
BGLY23
BLYS24
BTHR25
BTHR26
BPHE46
BASN135
BLYS136
BASP138
BMET139
BSER173
BALA174
BLEU175
BMG502
BHOH515
BHOH516
BHOH517
BHOH518
BHOH521
BHOH522
BHOH523
BHOH621

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 Residues6
DetailsBINDING:
ChainResidueDetails
AGLY18
AASP80
AASN135
BGLY18
BASP80
BASN135

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ASER1
BSER1

site_idSWS_FT_FI3
Number of Residues10
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS37
BLYS294
ALYS176
ALYS248
ALYS252
ALYS294
BLYS37
BLYS176
BLYS248
BLYS252

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ALYS56
BLYS56

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS313
BLYS313

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965
ChainResidueDetails
ATHR382
BTHR382

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 535
ChainResidueDetails
AASP21electrostatic stabiliser
ALYS24electrostatic stabiliser
ATHR25metal ligand
AHIS84electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 535
ChainResidueDetails
BASP21electrostatic stabiliser
BLYS24electrostatic stabiliser
BTHR25metal ligand
BHIS84electrostatic stabiliser

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PDB entries from 2024-04-24

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