1JRI
The Crystal Structure of an Sm-like Archaeal Protein with Two Heptamers in the Asymmetric Unit.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000398 | biological_process | mRNA splicing, via spliceosome |
| A | 0003723 | molecular_function | RNA binding |
| B | 0000398 | biological_process | mRNA splicing, via spliceosome |
| B | 0003723 | molecular_function | RNA binding |
| C | 0000398 | biological_process | mRNA splicing, via spliceosome |
| C | 0003723 | molecular_function | RNA binding |
| D | 0000398 | biological_process | mRNA splicing, via spliceosome |
| D | 0003723 | molecular_function | RNA binding |
| E | 0000398 | biological_process | mRNA splicing, via spliceosome |
| E | 0003723 | molecular_function | RNA binding |
| F | 0000398 | biological_process | mRNA splicing, via spliceosome |
| F | 0003723 | molecular_function | RNA binding |
| G | 0000398 | biological_process | mRNA splicing, via spliceosome |
| G | 0003723 | molecular_function | RNA binding |
| H | 0000398 | biological_process | mRNA splicing, via spliceosome |
| H | 0003723 | molecular_function | RNA binding |
| I | 0000398 | biological_process | mRNA splicing, via spliceosome |
| I | 0003723 | molecular_function | RNA binding |
| J | 0000398 | biological_process | mRNA splicing, via spliceosome |
| J | 0003723 | molecular_function | RNA binding |
| K | 0000398 | biological_process | mRNA splicing, via spliceosome |
| K | 0003723 | molecular_function | RNA binding |
| L | 0000398 | biological_process | mRNA splicing, via spliceosome |
| L | 0003723 | molecular_function | RNA binding |
| M | 0000398 | biological_process | mRNA splicing, via spliceosome |
| M | 0003723 | molecular_function | RNA binding |
| N | 0000398 | biological_process | mRNA splicing, via spliceosome |
| N | 0003723 | molecular_function | RNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL L 201 |
| Chain | Residue |
| L | SER21 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 101 |
| Chain | Residue |
| C | ALA17 |
| C | SER21 |
| C | ILE79 |
| D | THR68 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO L 102 |
| Chain | Residue |
| L | HOH212 |
| M | ASP44 |
| L | GLN12 |
| L | ARG13 |
| L | PRO14 |
| L | LEU15 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO E 103 |
| Chain | Residue |
| E | LYS41 |
| E | ASN52 |
| E | THR68 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO G 104 |
| Chain | Residue |
| G | ARG13 |
| G | PRO14 |
| G | LEU15 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO N 105 |
| Chain | Residue |
| N | LEU30 |
| N | LYS31 |
| N | ARG34 |
| N | HOH115 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO M 108 |
| Chain | Residue |
| F | VAL11 |
| M | VAL62 |
| M | ARG65 |
| M | HOH115 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO F 109 |
| Chain | Residue |
| F | ARG13 |
| F | PRO14 |
| F | LEU15 |
| F | GLU61 |
| G | ASP44 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO N 110 |
| Chain | Residue |
| H | THR68 |
| N | ALA17 |
| N | SER21 |
| N | ILE79 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO H 111 |
| Chain | Residue |
| H | LEU45 |
| I | ASP59 |
| N | GLN12 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO H 112 |
| Chain | Residue |
| C | ARG65 |
| H | ASP16 |
| H | GLY19 |
| H | ASN20 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO I 113 |
| Chain | Residue |
| B | ASN20 |
| I | ASN52 |
| I | ASP53 |
| I | GLY67 |
| I | THR68 |
