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 | 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 | 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 | 1990180 | biological_process | mitochondrial tRNA 3'-end processing |
B | 0000049 | molecular_function | tRNA 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 | 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 | 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: BINDING => ECO:0000250|UniProtKB:Q7SIB1 |
Chain | Residue | Details |
A | GLY38 | |
B | ARG125 | |
B | ASP168 | |
B | ARG171 | |
B | ARG174 | |
B | ARG177 | |
A | ARG41 | |
A | ARG125 | |
A | ASP168 | |
A | ARG171 | |
A | ARG174 | |
A | ARG177 | |
B | GLY38 | |
B | ARG41 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O66728 |
Chain | Residue | Details |
A | ASP51 | |
A | ASP53 | |
B | ASP51 | |
B | ASP53 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: May assist in discriminating ATP from CTP => ECO:0000250|UniProtKB:Q7SIB1 |
Chain | Residue | Details |
A | ASP126 | |
B | ASP126 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Involved in nucleotide selection => ECO:0000255 |
Chain | Residue | Details |
A | GLU167 | |
B | GLU167 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER374 | |
B | SER374 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS376 | |
B | LYS376 |