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5MI8

Structure of the phosphomimetic mutant of EF-Tu T383E

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 Residues6
Detailsbinding site for residue MG A 401
ChainResidue
ATHR26
AGDP403
AHOH507
AHOH513
AHOH528
AHOH535

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 402
ChainResidue
AHOH530
BGLU286
AASP355
AHOH503
AHOH520

site_idAC3
Number of Residues18
Detailsbinding site for residue GDP A 403
ChainResidue
AASP22
AHIS23
AGLY24
ALYS25
ATHR26
ATHR27
APHE47
AASN136
ALYS137
AASP139
ASER174
AALA175
ALEU176
AMG401
AHOH507
AHOH513
AHOH525
AHOH528

site_idAC4
Number of Residues3
Detailsbinding site for residue ACT A 404
ChainResidue
AARG124
AGLY127
APRO129

site_idAC5
Number of Residues6
Detailsbinding site for residue ACT A 405
ChainResidue
AMET113
APRO114
AARG117
AARG263
ALYS264
ALEU265

site_idAC6
Number of Residues1
Detailsbinding site for residue ACT A 406
ChainResidue
AASP208

site_idAC7
Number of Residues8
Detailsbinding site for residue EPE A 407
ChainResidue
ALEU266
AASP267
AGLU268
AGLY269
AARG270
AGLU273
AHOH504
AHOH531

site_idAC8
Number of Residues2
Detailsbinding site for residue BME A 408
ChainResidue
AARG289
BLYS264

site_idAC9
Number of Residues3
Detailsbinding site for residue BME A 409
ChainResidue
AASP162
BASP110
BPRO112

site_idAD1
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
BTHR26
BGDP403
BHOH502
BHOH503
BHOH506
BHOH539

site_idAD2
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
AHOH518
AHOH522
AHOH524
AHOH569
BHOH519
BHOH521

site_idAD3
Number of Residues18
Detailsbinding site for residue GDP B 403
ChainResidue
BASP22
BHIS23
BGLY24
BLYS25
BTHR26
BTHR27
BPHE47
BASN136
BLYS137
BASP139
BMET140
BSER174
BALA175
BLEU176
BMG401
BHOH502
BHOH503
BHOH506

site_idAD4
Number of Residues3
Detailsbinding site for residue ACT B 404
ChainResidue
BGLY84
BHIS85
BGLN115

site_idAD5
Number of Residues5
Detailsbinding site for residue EPE B 405
ChainResidue
BGLU268
BARG270
BGLU273
BHOH513
BHOH523

site_idAD6
Number of Residues4
Detailsbinding site for residue CL B 406
ChainResidue
BTHR72
BPRO73
BTHR74
BASP197

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
AGLU383
BGLU383

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

222624

PDB entries from 2024-07-17

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