1QMI
Crystal structure of RNA 3'-terminal phosphate cyclase, an ubiquitous enzyme with unusual topology
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0003963 | molecular_function | RNA-3'-phosphate cyclase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006396 | biological_process | RNA processing |
A | 0016874 | molecular_function | ligase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003963 | molecular_function | RNA-3'-phosphate cyclase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006396 | biological_process | RNA processing |
B | 0016874 | molecular_function | ligase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0003963 | molecular_function | RNA-3'-phosphate cyclase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006396 | biological_process | RNA processing |
C | 0016874 | molecular_function | ligase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0003963 | molecular_function | RNA-3'-phosphate cyclase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006396 | biological_process | RNA processing |
D | 0016874 | molecular_function | ligase activity |
Functional Information from PROSITE/UniProt
site_id | PS01287 |
Number of Residues | 11 |
Details | RTC RNA 3'-terminal phosphate cyclase signature. HGfyPaGGGvV |
Chain | Residue | Details |
A | HIS158-VAL168 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"20399182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QMH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20399182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KGD","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qmh |
Chain | Residue | Details |
A | HIS309 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qmh |
Chain | Residue | Details |
B | HIS309 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qmh |
Chain | Residue | Details |
C | HIS309 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qmh |
Chain | Residue | Details |
D | HIS309 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 882 |
Chain | Residue | Details |
A | SER22 | modifies pKa |
A | GLU329 | covalent catalysis |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 882 |
Chain | Residue | Details |
B | SER22 | modifies pKa |
B | GLU329 | covalent catalysis |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 882 |
Chain | Residue | Details |
C | SER22 | modifies pKa |
C | GLU329 | covalent catalysis |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 882 |
Chain | Residue | Details |
D | SER22 | modifies pKa |
D | GLU329 | covalent catalysis |