5MKO
[2Fe-2S] cluster containing TtuA in complex with AMP.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002098 | biological_process | tRNA wobble uridine modification |
| A | 0002143 | biological_process | tRNA wobble position uridine thiolation |
| A | 0002144 | cellular_component | cytosolic tRNA wobble base thiouridylase complex |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008033 | biological_process | tRNA processing |
| A | 0016740 | molecular_function | transferase activity |
| A | 0034227 | biological_process | tRNA thio-modification |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002098 | biological_process | tRNA wobble uridine modification |
| B | 0002143 | biological_process | tRNA wobble position uridine thiolation |
| B | 0002144 | cellular_component | cytosolic tRNA wobble base thiouridylase complex |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008033 | biological_process | tRNA processing |
| B | 0016740 | molecular_function | transferase activity |
| B | 0034227 | biological_process | tRNA thio-modification |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue AMP A 401 |
| Chain | Residue |
| A | ALA53 |
| A | GLY154 |
| A | HIS155 |
| A | HOH510 |
| A | VAL54 |
| A | SER55 |
| A | SER60 |
| A | LEU77 |
| A | ILE79 |
| A | LEU81 |
| A | LYS135 |
| A | THR153 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | CYS3 |
| A | CYS6 |
| A | CYS22 |
| A | HIS25 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 403 |
| Chain | Residue |
| A | CYS272 |
| A | CYS275 |
| A | CYS284 |
| A | CYS287 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FES A 404 |
| Chain | Residue |
| A | PRO127 |
| A | CYS128 |
| A | CYS131 |
| A | CYS220 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue AMP B 401 |
| Chain | Residue |
| B | ALA53 |
| B | VAL54 |
| B | SER55 |
| B | SER60 |
| B | LEU77 |
| B | ILE79 |
| B | LYS135 |
| B | THR153 |
| B | GLY154 |
| B | HIS155 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| B | CYS3 |
| B | CYS6 |
| B | CYS22 |
| B | HIS25 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 403 |
| Chain | Residue |
| B | CYS272 |
| B | CYS275 |
| B | CYS284 |
| B | CYS287 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue FES B 404 |
| Chain | Residue |
| B | CYS128 |
| B | CYS131 |
| B | CYS220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23444054","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28655838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VRH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28655838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
