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

2FX3

Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
ATHR25
AASP50
ACYS81
AGDP999

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GDP A 999
ChainResidue
ALYS24
ATHR25
ATHR26
APHE46
AASN135
ALYS136
AASP138
AMET139
ASER173
AALA174
ALEU175
AMG998
AHIS19
AVAL20
AASP21
AHIS22
AGLY23

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 Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118
ChainResidueDetails
AHIS19
ACYS81
ALYS136

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
AASP314

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AGLY18
AASP80
AASN135

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ASER1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ALYS56

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS313

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965
ChainResidueDetails
ATHR382

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
AHIS84

site_idMCSA1
Number of Residues4
DetailsM-CSA 535
ChainResidueDetails
AASP21electrostatic stabiliser
ALYS24electrostatic stabiliser
ATHR25metal ligand
AHIS84electrostatic stabiliser

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon