Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3B82

Structure of the eEF2-ExoA(E546H)-NAD+ complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003723	molecular_function	RNA binding
A	0003746	molecular_function	translation elongation factor activity
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006414	biological_process	translational elongation
A	0016787	molecular_function	hydrolase activity
A	0019843	molecular_function	rRNA binding
A	0042802	molecular_function	identical protein binding
A	0043022	molecular_function	ribosome binding
A	0045901	biological_process	positive regulation of translational elongation
A	0051087	molecular_function	protein-folding chaperone binding
A	1990145	biological_process	maintenance of translational fidelity
A	1990904	cellular_component	ribonucleoprotein complex
B	0047286	molecular_function	NAD+-diphthamide ADP-ribosyltransferase activity
C	0000166	molecular_function	nucleotide binding
C	0003723	molecular_function	RNA binding
C	0003746	molecular_function	translation elongation factor activity
C	0003924	molecular_function	GTPase activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006414	biological_process	translational elongation
C	0016787	molecular_function	hydrolase activity
C	0019843	molecular_function	rRNA binding
C	0042802	molecular_function	identical protein binding
C	0043022	molecular_function	ribosome binding
C	0045901	biological_process	positive regulation of translational elongation
C	0051087	molecular_function	protein-folding chaperone binding
C	1990145	biological_process	maintenance of translational fidelity
C	1990904	cellular_component	ribonucleoprotein complex
D	0047286	molecular_function	NAD+-diphthamide ADP-ribosyltransferase activity
E	0000166	molecular_function	nucleotide binding
E	0003723	molecular_function	RNA binding
E	0003746	molecular_function	translation elongation factor activity
E	0003924	molecular_function	GTPase activity
E	0005515	molecular_function	protein binding
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006412	biological_process	translation
E	0006414	biological_process	translational elongation
E	0016787	molecular_function	hydrolase activity
E	0019843	molecular_function	rRNA binding
E	0042802	molecular_function	identical protein binding
E	0043022	molecular_function	ribosome binding
E	0045901	biological_process	positive regulation of translational elongation
E	0051087	molecular_function	protein-folding chaperone binding
E	1990145	biological_process	maintenance of translational fidelity
E	1990904	cellular_component	ribonucleoprotein complex
F	0047286	molecular_function	NAD+-diphthamide ADP-ribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD B 700

Chain	Residue
B	HIS440
B	GLN460
B	TYR470
B	ILE471
B	ALA478
B	TYR481
B	GLU553
B	HOH728
B	HOH747
B	HOH777
B	HOH793
B	GLY441
B	THR442
B	ALA446
B	SER449
B	ILE450
B	GLY454
B	ARG456
B	ARG458

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD D 701

Chain	Residue
D	HIS440
D	GLY441
D	THR442
D	ALA446
D	SER449
D	ILE450
D	GLY454
D	ARG456
D	ARG458
D	GLN460
D	TYR470
D	ILE471
D	ALA478
D	TYR481
D	GLU553
D	HOH724
D	HOH730
D	HOH745
D	HOH809
D	HOH819

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD F 702

Chain	Residue
F	HIS440
F	GLY441
F	THR442
F	ALA446
F	SER449
F	ILE450
F	GLY454
F	ARG456
F	ARG458
F	GLN460
F	TYR470
F	ILE471
F	ALA478
F	TYR481
F	GLU553
F	HOH732
F	HOH772
F	HOH780
F	HOH784

Functional Information from PROSITE/UniProt

site_id	PS00301
Number of Residues	16
Details	G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT

Chain	Residue	Details
A	ASP58-THR73

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"N6-methyllysine; by EFM3; alternate","evidences":[{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25086354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"N6-methyllysine; by EFM2; alternate","evidences":[{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25086354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"Diphthamide","evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16950777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"721806","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PubMed","id":"2885323","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18583986","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	ASP29

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
C	ASP29

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
E	ASP29

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
B	GLU553

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
D	GLU553

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
F	GLU553

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	HIS108

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
C	HIS108

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
E	HIS108

site_id	MCSA1
Number of Residues	1
Details	M-CSA 769

Chain	Residue	Details
B	GLU553	electrostatic stabiliser

site_id	MCSA2
Number of Residues	1
Details	M-CSA 769

Chain	Residue	Details
D	GLU553	electrostatic stabiliser

site_id	MCSA3
Number of Residues	1
Details	M-CSA 769

Chain	Residue	Details
F	GLU553	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)