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4J0Q

Crystal structure of Pseudomonas putida elongation factor Tu (EF-Tu)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0097216molecular_functionguanosine tetraphosphate binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0097216molecular_functionguanosine tetraphosphate binding
C0003746molecular_functiontranslation elongation factor activity
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006414biological_processtranslational elongation
C0097216molecular_functionguanosine tetraphosphate binding
D0003746molecular_functiontranslation elongation factor activity
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0006414biological_processtranslational elongation
D0097216molecular_functionguanosine tetraphosphate binding
E0003746molecular_functiontranslation elongation factor activity
E0003924molecular_functionGTPase activity
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006412biological_processtranslation
E0006414biological_processtranslational elongation
E0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
ATHR26
AGDP402
AHOH513
AHOH541
AHOH542
AHOH543

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 402
ChainResidue
ALYS25
ATHR26
ATHR27
AASN136
ALYS137
AASP139
ALEU140
ASER174
AALA175
AARG176
AMG401
AHOH513
AHOH516
AHOH520
AHOH528
AHOH541
AHOH542
AHOH575
CHOH585
AASP22
AHIS23
AGLY24

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 403
ChainResidue
AARG176
AMET177
ALYS182
AASP184
AHOH549
CARG176
CLYS182
CASP184
CHOH548

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 404
ChainResidue
AGLY279
CASP110
CMET113

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 405
ChainResidue
AASP110
AHOH579
BMET264
BPHE265
BCYS278

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BTHR26
BGDP402
BHOH511
BHOH537
BHOH538
BHOH539

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP B 402
ChainResidue
BASP22
BHIS23
BGLY24
BLYS25
BTHR26
BTHR27
BASN136
BLYS137
BASP139
BLEU140
BSER174
BALA175
BARG176
BMG401
BHOH511
BHOH517
BHOH518
BHOH529
BHOH538
BHOH539

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES B 403
ChainResidue
BARG176
BMET177
BLYS182
BASP184
BHOH501
DARG176
DLYS182
DASP184
DHOH505

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
CTHR26
CGDP402
CHOH502
CHOH508
CHOH541
CHOH549

site_idBC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP C 402
ChainResidue
CMG401
CHOH502
CHOH516
CHOH521
CHOH541
CHOH549
CHOH566
CHOH580
CASP22
CHIS23
CGLY24
CLYS25
CTHR26
CTHR27
CASN136
CLYS137
CASP139
CLEU140
CSER174
CALA175
CARG176

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD C 403
ChainResidue
CTHR232
CGLU263
CPHE265
DASP110

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 401
ChainResidue
DTHR26
DGDP402
DHOH501
DHOH502
DHOH524
DHOH525

site_idBC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP D 402
ChainResidue
BHOH516
DASP22
DHIS23
DGLY24
DLYS25
DTHR26
DTHR27
DASN136
DLYS137
DASP139
DLEU140
DSER174
DALA175
DARG176
DMG401
DHOH502
DHOH510
DHOH524
DHOH529
DHOH534
DHOH556

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD D 403
ChainResidue
DTHR232
DGLU263
DASN277
DCYS278
EASP110

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 401
ChainResidue
ETHR26
EGDP402
EHOH501
EHOH509
EHOH510
EHOH511

site_idBC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GDP E 402
ChainResidue
EHIS20
EASP22
EHIS23
EGLY24
ELYS25
ETHR26
ETHR27
EASN136
ELYS137
EASP139
ELEU140
ESER174
EALA175
EARG176
EMG401
EHOH501
EHOH509
EHOH511

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES E 403
ChainResidue
EASP139
EASP139
EARG176
EASP184
EASP184

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD E 404
ChainResidue
BASP110
ETHR232

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DSapeEKaRGITIntA
ChainResidueDetails
AASP51-ALA66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118
ChainResidueDetails
AGLY19
DGLY19
DASP81
DASN136
EGLY19
EASP81
EASN136
AASP81
AASN136
BGLY19
BASP81
BASN136
CGLY19
CASP81
CASN136

225946

PDB entries from 2024-10-09

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