1ETU
STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY CRYSTALLOGRAPHY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion 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 | 0005886 | cellular_component | plasma membrane |
| A | 0006412 | biological_process | translation |
| A | 0006414 | biological_process | translational elongation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 394 |
| Chain | Residue |
| A | THR25 |
| A | GDP395 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GDP A 395 |
| Chain | Residue |
| A | MET139 |
| A | SER173 |
| A | ALA174 |
| A | LEU175 |
| A | MG394 |
| A | ASP21 |
| A | HIS22 |
| A | GLY23 |
| A | LYS24 |
| A | THR25 |
| A | THR26 |
| A | ASN135 |
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. DNapeEKaRGITIntS |
| Chain | Residue | Details |
| A | ASP50-SER65 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MI3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]} |
| 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 | ASP21 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | HIS84 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 535 |
| Chain | Residue | Details |
| A | ASP21 | electrostatic stabiliser |
| A | LYS24 | electrostatic stabiliser |
| A | THR25 | metal ligand |
| A | HIS84 | electrostatic stabiliser |
