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5OPD

Structure of phosphorylated EF-Tu in complex with GTP

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
B0003723molecular_functionRNA binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0032045cellular_componentguanyl-nucleotide exchange factor complex
B0046677biological_processresponse to antibiotic
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue IOD A 501
ChainResidue
AHIS85
AGLN115

site_idAC2
Number of Residues1
Detailsbinding site for residue IOD A 502
ChainResidue
ASER198

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD A 505
ChainResidue
AHIS320
ATHR321

site_idAC4
Number of Residues1
Detailsbinding site for residue IOD A 508
ChainResidue
AALA97

site_idAC5
Number of Residues1
Detailsbinding site for residue IOD A 514
ChainResidue
AARG280

site_idAC6
Number of Residues5
Detailsbinding site for residue MG A 515
ChainResidue
AHOH603
AHOH615
AHOH618
ATHR26
AGTP516

site_idAC7
Number of Residues21
Detailsbinding site for residue GTP A 516
ChainResidue
AHIS20
AVAL21
AASP22
AHIS23
AGLY24
ALYS25
ATHR26
ATHR27
APHE47
AASP51
AASN136
ALYS137
AASP139
AMET140
ASER174
AALA175
ALEU176
AMG515
AHOH603
AHOH615
AHOH649

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 519
ChainResidue
AGLU118
ALEU121
AGLU308
AASN356
AILE357
AHOH622

site_idAC9
Number of Residues1
Detailsbinding site for residue IOD B 501
ChainResidue
BHIS85

site_idAD1
Number of Residues1
Detailsbinding site for residue IOD B 503
ChainResidue
ALYS283

site_idAD2
Number of Residues1
Detailsbinding site for residue IOD B 504
ChainResidue
BSER198

site_idAD3
Number of Residues2
Detailsbinding site for residue IOD B 505
ChainResidue
BARG117
BHOH679

site_idAD4
Number of Residues2
Detailsbinding site for residue IOD B 506
ChainResidue
BARG319
BHIS320

site_idAD5
Number of Residues1
Detailsbinding site for residue IOD B 507
ChainResidue
BPHE324

site_idAD6
Number of Residues1
Detailsbinding site for residue IOD B 508
ChainResidue
BPHE262

site_idAD7
Number of Residues2
Detailsbinding site for residue IOD B 511
ChainResidue
BGLY225
BTHR257

site_idAD8
Number of Residues1
Detailsbinding site for residue IOD B 512
ChainResidue
BILE207

site_idAD9
Number of Residues3
Detailsbinding site for residue IOD B 513
ChainResidue
BARG234
BARG334
BHOH654

site_idAE1
Number of Residues2
Detailsbinding site for residue IOD B 514
ChainResidue
BARG334
BHOH654

site_idAE2
Number of Residues4
Detailsbinding site for residue MG B 515
ChainResidue
BTHR26
BCYS82
BGTP516
BHOH645

site_idAE3
Number of Residues20
Detailsbinding site for residue GTP B 516
ChainResidue
AARG328
BVAL21
BASP22
BHIS23
BGLY24
BLYS25
BTHR26
BTHR27
BASP51
BPRO83
BASN136
BLYS137
BASP139
BMET140
BSER174
BALA175
BLEU176
BMG515
BHOH611
BHOH616

site_idAE4
Number of Residues1
Detailsbinding site for residue NA B 517
ChainResidue
BASP267

site_idAE5
Number of Residues1
Detailsbinding site for residue NA B 518
ChainResidue
BGLU118

site_idAE6
Number of Residues2
Detailsbinding site for residue NA B 519
ChainResidue
BARG289
BASP337

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 Residues6
DetailsBINDING:
ChainResidueDetails
AGLY19
AASP81
AASN136
BGLY19
BASP81
BASN136

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI3
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
ALYS57
BLYS57

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS314
BLYS314

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965
ChainResidueDetails
ATPO383
BTPO383

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 535
ChainResidueDetails
AASP22electrostatic stabiliser
ALYS25electrostatic stabiliser
ATHR26metal ligand
AHIS85electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 535
ChainResidueDetails
BASP22electrostatic stabiliser
BLYS25electrostatic stabiliser
BTHR26metal ligand
BHIS85electrostatic stabiliser

222415

PDB entries from 2024-07-10

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