3H1C
Crystal structure of Polynucleotide Phosphorylase (PNPase) core bound to RNase E and Tungstate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| A | 0006396 | biological_process | RNA processing |
| A | 0006402 | biological_process | mRNA catabolic process |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| B | 0006396 | biological_process | RNA processing |
| B | 0006402 | biological_process | mRNA catabolic process |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| C | 0006396 | biological_process | RNA processing |
| C | 0006402 | biological_process | mRNA catabolic process |
| G | 0003723 | molecular_function | RNA binding |
| G | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| G | 0006396 | biological_process | RNA processing |
| G | 0006402 | biological_process | mRNA catabolic process |
| I | 0003723 | molecular_function | RNA binding |
| I | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| I | 0006396 | biological_process | RNA processing |
| I | 0006402 | biological_process | mRNA catabolic process |
| K | 0003723 | molecular_function | RNA binding |
| K | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| K | 0006396 | biological_process | RNA processing |
| K | 0006402 | biological_process | mRNA catabolic process |
| M | 0003723 | molecular_function | RNA binding |
| M | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| M | 0006396 | biological_process | RNA processing |
| M | 0006402 | biological_process | mRNA catabolic process |
| O | 0003723 | molecular_function | RNA binding |
| O | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| O | 0006396 | biological_process | RNA processing |
| O | 0006402 | biological_process | mRNA catabolic process |
| R | 0003723 | molecular_function | RNA binding |
| R | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| R | 0006396 | biological_process | RNA processing |
| R | 0006402 | biological_process | mRNA catabolic process |
| T | 0003723 | molecular_function | RNA binding |
| T | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| T | 0006396 | biological_process | RNA processing |
| T | 0006402 | biological_process | mRNA catabolic process |
| V | 0003723 | molecular_function | RNA binding |
| V | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| V | 0006396 | biological_process | RNA processing |
| V | 0006402 | biological_process | mRNA catabolic process |
| X | 0003723 | molecular_function | RNA binding |
| X | 0004654 | molecular_function | polyribonucleotide nucleotidyltransferase activity |
| X | 0006396 | biological_process | RNA processing |
| X | 0006402 | biological_process | mRNA catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE WO4 A 550 |
| Chain | Residue |
| A | HIS403 |
| A | SER434 |
| A | GLY436 |
| A | SER437 |
| A | SER438 |
| A | SER439 |
| A | LYS494 |
| A | WO4551 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE WO4 A 551 |
| Chain | Residue |
| A | ASP492 |
| A | LYS494 |
| A | GLN506 |
| A | ASP508 |
| A | WO4550 |
| A | HIS403 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE WO4 B 550 |
| Chain | Residue |
| B | ARG399 |
| B | HIS403 |
| B | SER434 |
| B | GLY436 |
| B | SER437 |
| B | SER438 |
| B | SER439 |
| B | LYS494 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 B 551 |
| Chain | Residue |
| B | ARG93 |
| B | ARG97 |
| B | ARG399 |
| B | HIS403 |
| B | ASP508 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE WO4 C 550 |
| Chain | Residue |
| C | ARG399 |
| C | HIS403 |
| C | SER434 |
| C | GLY436 |
| C | SER437 |
| C | SER438 |
| C | ASP486 |
| C | LYS494 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE WO4 G 550 |
| Chain | Residue |
| G | ARG399 |
| G | HIS403 |
| G | GLY436 |
| G | SER437 |
| G | SER438 |
| G | SER439 |
| G | ASP486 |
| G | LYS494 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 I 550 |
| Chain | Residue |
| I | HIS403 |
| I | GLY436 |
| I | SER438 |
| I | SER439 |
| I | LYS494 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE WO4 K 550 |
| Chain | Residue |
| K | SER434 |
| K | GLY436 |
| K | SER438 |
| K | SER439 |
| K | ASP486 |
| K | LYS494 |
| K | WO4551 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 K 551 |
| Chain | Residue |
| K | ARG93 |
| K | ARG399 |
| K | HIS403 |
| K | ASP508 |
| K | WO4550 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE WO4 M 550 |
| Chain | Residue |
| M | SER437 |
| M | SER438 |
| M | WO4551 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 M 551 |
| Chain | Residue |
| M | ARG399 |
| M | ASP492 |
| M | GLN506 |
| M | ASP508 |
| M | WO4550 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE WO4 O 550 |
| Chain | Residue |
| O | ARG93 |
| O | ARG399 |
| O | HIS403 |
| O | ASP508 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 O 551 |
| Chain | Residue |
| O | HIS403 |
| O | GLY436 |
| O | SER438 |
| O | SER439 |
| O | LYS494 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE WO4 R 550 |
| Chain | Residue |
| R | HIS403 |
| R | SER437 |
| R | SER438 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 R 551 |
| Chain | Residue |
| R | ARG93 |
| R | ARG399 |
| R | HIS403 |
| R | ASP492 |
| R | ASP508 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE WO4 T 550 |
| Chain | Residue |
| T | ARG93 |
| T | ARG399 |
| T | HIS403 |
| T | ASP508 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE WO4 T 551 |
| Chain | Residue |
| T | HIS403 |
| T | SER437 |
| T | ASP486 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 V 550 |
| Chain | Residue |
| V | HIS403 |
| V | GLY436 |
| V | SER437 |
| V | SER438 |
| V | WO4551 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE WO4 V 551 |
| Chain | Residue |
| V | ASP508 |
| V | WO4550 |
| V | ARG93 |
| V | GLN506 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE WO4 X 550 |
| Chain | Residue |
| X | TYR380 |
| X | HIS403 |
| X | GLY436 |
| X | SER437 |
| X | SER438 |
| X | SER439 |
| X | WO4551 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE WO4 X 551 |
| Chain | Residue |
| X | ARG93 |
| X | ARG399 |
| X | HIS403 |
| X | ASP508 |
| X | WO4550 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19327365 |
| Chain | Residue | Details |
| A | ASP486 | |
| I | ASP492 | |
| K | ASP486 | |
| K | ASP492 | |
| M | ASP486 | |
| M | ASP492 | |
| O | ASP486 | |
| O | ASP492 | |
| R | ASP486 | |
| R | ASP492 | |
| T | ASP486 | |
| A | ASP492 | |
| T | ASP492 | |
| V | ASP486 | |
| V | ASP492 | |
| X | ASP486 | |
| X | ASP492 | |
| B | ASP486 | |
| B | ASP492 | |
| C | ASP486 | |
| C | ASP492 | |
| G | ASP486 | |
| G | ASP492 | |
| I | ASP486 |
