4X4W
Crystal structure of the full-length human mitochondrial CCA-adding enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001680 | biological_process | tRNA 3'-terminal CCA addition |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004810 | molecular_function | CCA tRNA nucleotidyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006396 | biological_process | RNA processing |
| A | 0008033 | biological_process | tRNA processing |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| A | 0042780 | biological_process | tRNA 3'-end processing |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0072344 | biological_process | rescue of stalled ribosome |
| A | 0106354 | biological_process | tRNA surveillance |
| A | 0160016 | molecular_function | CCACCA tRNA nucleotidyltransferase activity |
| A | 1902494 | cellular_component | catalytic complex |
| A | 1990180 | biological_process | mitochondrial tRNA 3'-end processing |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001680 | biological_process | tRNA 3'-terminal CCA addition |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004810 | molecular_function | CCA tRNA nucleotidyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006396 | biological_process | RNA processing |
| B | 0008033 | biological_process | tRNA processing |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| B | 0042780 | biological_process | tRNA 3'-end processing |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0072344 | biological_process | rescue of stalled ribosome |
| B | 0106354 | biological_process | tRNA surveillance |
| B | 0160016 | molecular_function | CCACCA tRNA nucleotidyltransferase activity |
| B | 1902494 | cellular_component | catalytic complex |
| B | 1990180 | biological_process | mitochondrial tRNA 3'-end processing |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 500 |
| Chain | Residue |
| A | PRO186 |
| A | HIS224 |
| A | ASN226 |
| A | HIS227 |
| A | HOH760 |
| A | HOH807 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue FLC A 501 |
| Chain | Residue |
| A | ARG177 |
| A | LYS218 |
| A | HOH771 |
| A | GLY38 |
| A | ARG41 |
| A | ARG174 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ARG100 |
| A | ARG124 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ARG368 |
| A | SER373 |
| B | SER21 |
| B | HIS90 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | LYS291 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | SER208 |
| A | HOH660 |
| A | HOH950 |
| A | HOH955 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | MET4 |
| A | HOH647 |
| A | HOH728 |
| A | HOH838 |
| A | HOH908 |
| A | HOH956 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | HOH654 |
| A | HOH666 |
| A | HOH964 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 508 |
| Chain | Residue |
| A | ARG386 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 509 |
| Chain | Residue |
| A | ARG88 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 510 |
| Chain | Residue |
| A | HOH1004 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 500 |
| Chain | Residue |
| A | HOH1018 |
| B | PRO186 |
| B | HIS224 |
| B | ASN226 |
| B | HIS227 |
| B | HOH761 |
| B | HOH778 |
| B | HOH915 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue FLC B 501 |
| Chain | Residue |
| B | GLY38 |
| B | ARG41 |
| B | ASN130 |
| B | ARG174 |
| B | ARG177 |
| B | PHE178 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ARG100 |
| B | ARG124 |
| B | ARG125 |
| B | HOH769 |
| B | HOH950 |
| B | HOH960 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| A | LYS369 |
| B | ARG73 |
| B | ARG88 |
| B | GLU91 |
| B | HOH613 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| A | HIS365 |
| A | ARG368 |
| B | ARG73 |
| B | LEU89 |
| B | HIS90 |
| B | HOH610 |
| B | HOH613 |
| B | HOH634 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | HOH977 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| A | SER374 |
| A | GLY375 |
| A | LYS376 |
| B | LYS28 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | THR115 |
| B | THR116 |
| B | HOH660 |
| B | HOH668 |
| B | HOH831 |
| B | HOH850 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 508 |
| Chain | Residue |
| B | PHE360 |
| B | ARG386 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 509 |
| Chain | Residue |
| B | SER208 |
| B | HOH905 |
| B | HOH982 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7SIB1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O66728","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"May assist in discriminating ATP from CTP","evidences":[{"source":"UniProtKB","id":"Q7SIB1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in nucleotide selection","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
