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1HA3

ELONGATION FACTOR TU IN COMPLEX WITH aurodox

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 407
ChainResidue
ATHR25
AGDP406
AHOH2018
AHOH2043
AHOH2258
AHOH2260

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 407
ChainResidue
BHOH2051
BHOH2311
BHOH2319
BTHR25
BGDP406
BHOH2019

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 406
ChainResidue
AASP21
AHIS22
AGLY23
ALYS24
ATHR25
ATHR26
ATYR47
AASN136
ALYS137
AASP139
AMET140
ASER174
AALA175
ALEU176
AMG407
AHOH2083
AHOH2258
AHOH2259
AHOH2260
AHOH2261
AHOH2262
AHOH2263

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE MAU A 408
ChainResidue
AILE93
AARG117
ALEU121
AARG124
AGLN125
AVAL126
ATYR161
AGLU162
ATYR321
AGLU326
AGLU327
AARG345
AARG385
APHE386
AALA387
AALA397
AHOH2077
AHOH2199
AHOH2252
AHOH2264
AHOH2265
AHOH2266
AHOH2267
AHOH2268
AHOH2269
BARG330
BHIS331

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 482
ChainResidue
AVAL80
ACYS82
APRO83
AASN91
AMET92
AHOH2271

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP B 406
ChainResidue
BASP21
BHIS22
BGLY23
BLYS24
BTHR25
BTHR26
BASN136
BLYS137
BASP139
BMET140
BSER174
BALA175
BLEU176
BMG407
BHOH2108
BHOH2311
BHOH2312
BHOH2313
BHOH2314
BHOH2315
BHOH2316
BHOH2317
BHOH2318
BHOH2319

site_idAC7
Number of Residues28
DetailsBINDING SITE FOR RESIDUE MAU B 408
ChainResidue
BTYR161
BGLU162
BTYR321
BGLU326
BGLU327
BARG345
BARG385
BPHE386
BALA387
BALA397
BHOH2097
BHOH2298
BHOH2307
BHOH2320
BHOH2321
BHOH2322
BHOH2323
BHOH2324
BHOH2325
BHOH2326
AARG330
AHIS331
AHOH2201
BILE93
BGLU118
BLEU121
BARG124
BGLN125

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BME B 482
ChainResidue
BVAL80
BCYS82
BPRO83
BASN91
BMET92
BHOH2054
BHOH2327

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsRegion: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsRegion: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsRegion: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11278992","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HA3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2C78","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V5G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V5P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V5Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V5S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V8Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PDB","id":"2C78","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0CE47","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AASP21

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BASP21

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS85

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BHIS85

243911

PDB entries from 2025-10-29

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