Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0004792 | molecular_function | thiosulfate-cyanide sulfurtransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0008097 | molecular_function | 5S rRNA binding |
A | 0016740 | molecular_function | transferase activity |
A | 0016783 | molecular_function | sulfurtransferase activity |
A | 0016784 | molecular_function | 3-mercaptopyruvate sulfurtransferase activity |
A | 0035928 | biological_process | rRNA import into mitochondrion |
A | 0051029 | biological_process | rRNA transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 297 |
Chain | Residue |
A | ARG182 |
A | CYS247 |
A | ARG248 |
A | LYS249 |
A | GLY250 |
A | VAL251 |
A | THR252 |
Functional Information from PROSITE/UniProt
site_id | PS00380 |
Number of Residues | 12 |
Details | RHODANESE_1 Rhodanese signature 1. YlerHVPGAsfF |
Chain | Residue | Details |
A | TYR47-PHE58 | |
site_id | PS00683 |
Number of Residues | 11 |
Details | RHODANESE_2 Rhodanese C-terminal signature. VaiYDGSWfEW |
Chain | Residue | Details |
A | VAL268-TRP278 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 118 |
Details | Domain: {"description":"Rhodanese 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 115 |
Details | Domain: {"description":"Rhodanese 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 15 |
Details | Region: {"description":"Hinge"} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"711738","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Binding site: {} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24329","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52196","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52196","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rhs |
Chain | Residue | Details |
A | LYS249 | |
A | ARG186 | |
A | ARG248 | |
A | VAL251 | |
A | THR252 | |
A | GLY250 | |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 153 |
Chain | Residue | Details |
A | ARG186 | electrostatic stabiliser, hydrogen bond donor |
A | CYS247 | nucleofuge, nucleophile |
A | ARG248 | electrostatic stabiliser, hydrogen bond donor |
A | LYS249 | electrostatic stabiliser |
A | GLY250 | electrostatic stabiliser, hydrogen bond donor |
A | VAL251 | electrostatic stabiliser, hydrogen bond donor |
A | THR252 | electrostatic stabiliser, hydrogen bond donor |
A | SER274 | electrostatic stabiliser |