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6EZE

The open conformation of E.coli Elongation Factor Tu in complex with GDPNP.

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 Residues20
Detailsbinding site for residue GNP A 401
ChainResidue
AVAL20
AASP138
AMET139
ASER173
AALA174
ALEU175
AMG402
AHOH511
AHOH515
AHOH517
AHOH542
AASP21
AHOH603
AHIS22
AGLY23
ALYS24
ATHR25
ATHR26
AASN135
ALYS136

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 402
ChainResidue
ATHR25
AGNP401
AHOH511
AHOH515
AHOH517

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
AARG288
AARG377
AHOH522
AHOH577

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AASP165
AASP166
ATHR167
AHOH557

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 405
ChainResidue
AGLU183
ATRP184

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 406
ChainResidue
ALEU120
AGLU307
AASN355
AHOH520

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 A 407
ChainResidue
AMET260
APHE261
AARG262
ALYS263
BARG288

site_idAC8
Number of Residues5
Detailsbinding site for residue PEG A 408
ChainResidue
ALEU211
AARG233
AARG333
AASP369
ALEU372

site_idAC9
Number of Residues5
Detailsbinding site for residue PEG A 409
ChainResidue
APRO111
AMET112
APRO113
AARG116
AHOH531

site_idAD1
Number of Residues3
Detailsbinding site for residue PEG A 410
ChainResidue
AHIS84
AALA85
AGLN114

site_idAD2
Number of Residues21
Detailsbinding site for residue GNP B 401
ChainResidue
BVAL20
BASP21
BHIS22
BGLY23
BLYS24
BTHR25
BTHR26
BPHE46
BASN135
BLYS136
BASP138
BMET139
BSER173
BALA174
BLEU175
BMG402
BHOH510
BHOH528
BHOH555
BHOH574
BHOH585

site_idAD3
Number of Residues5
Detailsbinding site for residue MG B 402
ChainResidue
BTHR25
BGNP401
BHOH510
BHOH528
BHOH555

site_idAD4
Number of Residues3
Detailsbinding site for residue GOL B 403
ChainResidue
BARG318
BTYR326
BHOH503

site_idAD5
Number of Residues3
Detailsbinding site for residue GOL B 404
ChainResidue
BTYR331
BARG333
BARG373

site_idAD6
Number of Residues2
Detailsbinding site for residue GOL B 405
ChainResidue
BARG327
BTHR338

site_idAD7
Number of Residues2
Detailsbinding site for residue GOL B 406
ChainResidue
AARG283
BARG262

site_idAD8
Number of Residues6
Detailsbinding site for residue SO4 B 407
ChainResidue
AARG288
BMET260
BPHE261
BARG262
BLYS263
BHOH543

site_idAD9
Number of Residues4
Detailsbinding site for residue SO4 B 408
ChainResidue
BPRO111
BMET112
BPRO113
BARG116

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-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS313
BLYS313

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965
ChainResidueDetails
ATHR382
BTHR382

218853

PDB entries from 2024-04-24

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