2NPF
Structure of eEF2 in complex with moriniafungin
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 | 0003746 | molecular_function | translation elongation factor activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006414 | biological_process | translational elongation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019843 | molecular_function | rRNA binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043022 | molecular_function | ribosome binding |
| B | 0045901 | biological_process | positive regulation of translational elongation |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 1990145 | biological_process | maintenance of translational fidelity |
| B | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MOU A 901 |
| Chain | Residue |
| A | PRO487 |
| A | ALA562 |
| A | PRO727 |
| A | VAL774 |
| A | SER777 |
| A | GLY779 |
| A | PHE780 |
| A | THR781 |
| A | MET796 |
| A | VAL797 |
| A | PHE798 |
| A | VAL488 |
| A | TRP801 |
| A | GLN490 |
| A | LEU519 |
| A | TYR521 |
| A | SER523 |
| A | GLU524 |
| A | VAL560 |
| A | VAL561 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MOU B 1901 |
| Chain | Residue |
| B | VAL488 |
| B | GLN490 |
| B | LEU519 |
| B | TYR521 |
| B | SER523 |
| B | GLU524 |
| B | VAL560 |
| B | VAL561 |
| B | ALA562 |
| B | PRO727 |
| B | PHE729 |
| B | SER777 |
| B | GLY779 |
| B | PHE780 |
| B | THR781 |
| B | MET796 |
| B | PHE798 |
| B | TRP801 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GDP A 902 |
| Chain | Residue |
| A | HIS27 |
| A | ASP29 |
| A | HIS30 |
| A | GLY31 |
| A | LYS32 |
| A | SER33 |
| A | THR34 |
| A | ASN158 |
| A | LYS159 |
| A | ASP161 |
| A | SER213 |
| A | GLY214 |
| A | LEU215 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GDP B 1902 |
| Chain | Residue |
| B | HIS27 |
| B | VAL28 |
| B | ASP29 |
| B | HIS30 |
| B | GLY31 |
| B | LYS32 |
| B | SER33 |
| B | THR34 |
| B | ASN158 |
| B | LYS159 |
| B | ASP161 |
| B | SER213 |
| B | GLY214 |
| B | LEU215 |
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 | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2NPF |
| Chain | Residue | Details |
| A | ALA26 | |
| B | ALA26 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2E1R, ECO:0007744|PDB:2NPF |
| Chain | Residue | Details |
| A | ASN158 | |
| A | SER213 | |
| B | ASN158 | |
| B | SER213 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354 |
| Chain | Residue | Details |
| A | LYS509 | |
| B | LYS509 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER579 | |
| B | SER579 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354 |
| Chain | Residue | Details |
| A | LYS613 | |
| B | LYS613 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806 |
| Chain | Residue | Details |
| A | HIS699 | |
| B | HIS699 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | THR713 | |
| A | THR763 | |
| B | THR713 | |
| B | THR763 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
| Chain | Residue | Details |
| A | LYS841 | |
| B | 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 |
| B | ASP29 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | HIS108 |
