3B82
Structure of the eEF2-ExoA(E546H)-NAD+ complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:2885323 |
Chain | Residue | Details |
B | GLU553 | |
D | GLU553 | |
F | GLU553 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18583986 |
Chain | Residue | Details |
B | HIS440 | |
F | SER449 | |
F | GLY454 | |
F | GLU553 | |
B | SER449 | |
B | GLY454 | |
B | GLU553 | |
D | HIS440 | |
D | SER449 | |
D | GLY454 | |
D | GLU553 | |
F | HIS440 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354 |
Chain | Residue | Details |
A | LYS509 | |
C | LYS509 | |
E | LYS509 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER579 | |
C | SER579 | |
E | SER579 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354 |
Chain | Residue | Details |
A | LYS613 | |
C | LYS613 | |
E | LYS613 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | MOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806 |
Chain | Residue | Details |
A | DDE699 | |
C | DDE699 | |
E | DDE699 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | THR713 | |
A | THR763 | |
C | THR713 | |
C | THR763 | |
E | THR713 | |
E | THR763 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
A | LYS841 | |
C | LYS841 | |
E | LYS841 |
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 |