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1ZM9

Structure of eEF2-ETA in complex with PJ34

Functional Information from GO Data
ChainGOidnamespacecontents
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016787molecular_functionhydrolase activity
A0019843molecular_functionrRNA binding
A0042802molecular_functionidentical protein binding
A0043022molecular_functionribosome binding
A0045901biological_processpositive regulation of translational elongation
A0051087molecular_functionprotein-folding chaperone binding
A1990145biological_processmaintenance of translational fidelity
A1990904cellular_componentribonucleoprotein complex
B0047286molecular_functionNAD+-diphthamide ADP-ribosyltransferase activity
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
D0047286molecular_functionNAD+-diphthamide ADP-ribosyltransferase activity
E0003746molecular_functiontranslation elongation factor activity
E0003924molecular_functionGTPase activity
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006412biological_processtranslation
E0006414biological_processtranslational elongation
E0016787molecular_functionhydrolase activity
E0019843molecular_functionrRNA binding
E0042802molecular_functionidentical protein binding
E0043022molecular_functionribosome binding
E0045901biological_processpositive regulation of translational elongation
E0051087molecular_functionprotein-folding chaperone binding
E1990145biological_processmaintenance of translational fidelity
E1990904cellular_componentribonucleoprotein complex
F0047286molecular_functionNAD+-diphthamide ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE P34 B 700
ChainResidue
BHIS440
BGLY441
BTYR470
BILE471
BALA478
BTYR481

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE P34 D 701
ChainResidue
DALA478
DTYR481
DHIS440
DGLY441
DTYR470

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE P34 F 702
ChainResidue
FHIS440
FGLY441
FTYR470
FILE471
FALA478
FTYR481
FGLU553

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT
ChainResidueDetails
AASP58-THR73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2885323
ChainResidueDetails
BGLU553
DGLU553
FGLU553

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:18583986
ChainResidueDetails
BHIS440
FSER449
FGLY454
FGLU553
BSER449
BGLY454
BGLU553
DHIS440
DSER449
DGLY454
DGLU553
FHIS440

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354
ChainResidueDetails
ALYS509
CLYS509
ELYS509

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER579
CSER579
ESER579

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354
ChainResidueDetails
ALYS613
CLYS613
ELYS613

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806
ChainResidueDetails
ADDE699
CDDE699
EDDE699

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR713
ATHR763
CTHR713
CTHR763
ETHR713
ETHR763

site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS841
CLYS841
ELYS841

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AASP29

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CASP29

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
EASP29

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BGLU553

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DGLU553

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
FGLU553

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS108

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CHIS108

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
EHIS108

site_idMCSA1
Number of Residues1
DetailsM-CSA 769
ChainResidueDetails
BGLU553electrostatic stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 769
ChainResidueDetails
DGLU553electrostatic stabiliser

site_idMCSA3
Number of Residues1
DetailsM-CSA 769
ChainResidueDetails
FGLU553electrostatic stabiliser

226707

PDB entries from 2024-10-30

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