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3DNY

Fitting of the eEF2 crystal structure into the cryo-EM density map of the eEF2.80S.AlF4-.GDP complex

Functional Information from GO Data
ChainGOidnamespacecontents
T0003746molecular_functiontranslation elongation factor activity
T0003924molecular_functionGTPase activity
T0005515molecular_functionprotein binding
T0005525molecular_functionGTP binding
T0005737cellular_componentcytoplasm
T0005829cellular_componentcytosol
T0006412biological_processtranslation
T0006414biological_processtranslational elongation
T0016787molecular_functionhydrolase activity
T0019843molecular_functionrRNA binding
T0042802molecular_functionidentical protein binding
T0043022molecular_functionribosome binding
T0045901biological_processpositive regulation of translational elongation
T0051087molecular_functionprotein-folding chaperone binding
T1990145biological_processmaintenance of translational fidelity
T1990904cellular_componentribonucleoprotein complex
Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT
ChainResidueDetails
TASP58-THR73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2NPF
ChainResidueDetails
TALA26

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2E1R, ECO:0007744|PDB:2NPF
ChainResidueDetails
TASN158
TSER213

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354
ChainResidueDetails
TLYS509

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
TSER579

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354
ChainResidueDetails
TLYS613

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806
ChainResidueDetails
THIS699

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
TTHR713
TTHR763

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
TLYS841

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
TASP29

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
THIS108

222415

PDB entries from 2024-07-10

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