Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5MI9

Structure of the phosphomimetic mutant of the elongation factor EF-Tu T62E

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016020cellular_componentmembrane
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0097216molecular_functionguanosine tetraphosphate binding
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0016020cellular_componentmembrane
B0032045cellular_componentguanyl-nucleotide exchange factor complex
B0046677biological_processresponse to antibiotic
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 401
ChainResidue
ATHR26
AGDP402
AHOH501
AHOH502
AHOH505

site_idAC2
Number of Residues14
Detailsbinding site for residue GDP A 402
ChainResidue
ALYS25
ATHR26
ATHR27
APHE47
ALYS137
ASER174
AALA175
ALEU176
AMG401
AHOH502
AHIS20
AASP22
AHIS23
AGLY24

site_idAC3
Number of Residues4
Detailsbinding site for residue MG B 401
ChainResidue
BTHR26
BGDP402
BHOH503
BHOH504

site_idAC4
Number of Residues18
Detailsbinding site for residue GDP B 402
ChainResidue
BHIS20
BVAL21
BASP22
BHIS23
BGLY24
BLYS25
BTHR26
BTHR27
BPHE47
BASN136
BLYS137
BASP139
BSER174
BALA175
BLEU176
BMG401
BHOH503
BHOH504

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
ATHR383
BTHR383

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon