Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BVN

E. coli EF-Tu:GDPNP in complex with the antibiotic enacyloxin IIa

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
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
A0016787molecular_functionhydrolase activity
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion 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
B0016787molecular_functionhydrolase activity
B0032045cellular_componentguanyl-nucleotide exchange factor complex
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1395
ChainResidue
ATHR25
AGNP1394
AHOH2003
AHOH2004

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B1395
ChainResidue
BTHR25
BGNP1394
BHOH2005
BHOH2006
BHOH2007

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GNP A1394
ChainResidue
AVAL20
AASP21
AHIS22
AGLY23
ALYS24
ATHR25
ATHR26
APRO82
AGLY83
AASN135
ALYS136
AASP138
AMET139
ASER173
AALA174
ALEU175
AMG1395
AHOH2003
AHOH2004
AHOH2082

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ENX A1396
ChainResidue
AALA96
ALEU120
AARG123
AGLN124
AVAL125
AGLN159
ATYR160
ALEU311
ALYS313
AASP314
AGLU315
ATYR331
AARG333
AARG373
APHE374
AALA375
AHOH2081
AHOH2083

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GNP B1394
ChainResidue
BVAL20
BASP21
BHIS22
BGLY23
BLYS24
BTHR25
BTHR26
BPRO82
BGLY83
BASN135
BLYS136
BASP138
BMET139
BSER173
BALA174
BLEU175
BMG1395
BHOH2005
BHOH2007
BHOH2095

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ENX B1396
ChainResidue
BALA96
BLEU120
BARG123
BGLN124
BVAL125
BGLN159
BTYR160
BLEU311
BLYS313
BASP314
BGLU315
BARG333
BARG373
BPHE374
BALA375
BHOH2097

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 Residues14
DetailsRegion: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsRegion: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsRegion: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsRegion: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues28
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues10
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"2022614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"389663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6997043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7021545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000305"}]}
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
AHIS84

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BHIS84

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon