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1N0V

Crystal structure of elongation factor 2

Functional Information from GO Data
ChainGOidnamespacecontents
C0003746molecular_functiontranslation elongation factor activity
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006414biological_processtranslational elongation
C0016787molecular_functionhydrolase activity
C0019843molecular_functionrRNA binding
C0042802molecular_functionidentical protein binding
C0043022molecular_functionribosome binding
C0045901biological_processpositive regulation of translational elongation
C0051087molecular_functionprotein-folding chaperone binding
C1990145biological_processmaintenance of translational fidelity
C1990904cellular_componentribonucleoprotein complex
D0003746molecular_functiontranslation elongation factor activity
D0003924molecular_functionGTPase activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0006414biological_processtranslational elongation
D0016787molecular_functionhydrolase activity
D0019843molecular_functionrRNA binding
D0042802molecular_functionidentical protein binding
D0043022molecular_functionribosome binding
D0045901biological_processpositive regulation of translational elongation
D0051087molecular_functionprotein-folding chaperone binding
D1990145biological_processmaintenance of translational fidelity
D1990904cellular_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
CASP58-THR73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2NPF
ChainResidueDetails
CALA26
DALA26

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2E1R, ECO:0007744|PDB:2NPF
ChainResidueDetails
CASN158
CSER213
DASN158
DSER213

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354
ChainResidueDetails
CLYS509
DLYS509

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
CSER579
DSER579

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354
ChainResidueDetails
CLYS613
DLYS613

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806
ChainResidueDetails
CHIS699
DHIS699

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
CTHR713
CTHR763
DTHR713
DTHR763

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
CLYS841
DLYS841

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CASP29

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DASP29

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CHIS108

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DHIS108

224201

PDB entries from 2024-08-28

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