5ULJ
Crystal structure of Scheffersomyces stipitis Rai1 in complex with (3'-NADP)+ and calcium ion
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006397 | biological_process | mRNA processing |
| A | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0110155 | biological_process | NAD-cap decapping |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006397 | biological_process | mRNA processing |
| B | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0110155 | biological_process | NAD-cap decapping |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0005829 | cellular_component | cytosol |
| C | 0006397 | biological_process | mRNA processing |
| C | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0110155 | biological_process | NAD-cap decapping |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0005829 | cellular_component | cytosol |
| D | 0006397 | biological_process | mRNA processing |
| D | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0110155 | biological_process | NAD-cap decapping |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | GLU179 |
| A | ASP230 |
| A | GLU249 |
| A | LEU250 |
| A | 0WD402 |
| A | HOH504 |
| A | HOH505 |
| A | HOH512 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 0WD A 402 |
| Chain | Residue |
| A | MET77 |
| A | TYR107 |
| A | ARG108 |
| A | GLY109 |
| A | TYR176 |
| A | GLN209 |
| A | ALA226 |
| A | GLY227 |
| A | GLU228 |
| A | LYS251 |
| A | GLN275 |
| A | CA401 |
| A | HOH522 |
| A | HOH543 |
| A | HOH669 |
| A | ASN76 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 401 |
| Chain | Residue |
| B | ASP230 |
| B | GLU249 |
| B | LEU250 |
| B | 0WD402 |
| B | HOH521 |
| B | HOH540 |
| B | HOH604 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | binding site for residue 0WD B 402 |
| Chain | Residue |
| B | GLU73 |
| B | ASN76 |
| B | MET77 |
| B | TYR107 |
| B | ARG108 |
| B | GLY109 |
| B | SER140 |
| B | GLU145 |
| B | TYR176 |
| B | ASN206 |
| B | GLN209 |
| B | GLY227 |
| B | GLU228 |
| B | GLU249 |
| B | LYS251 |
| B | CA401 |
| B | HOH503 |
| B | HOH506 |
| B | HOH520 |
| B | HOH521 |
| B | HOH525 |
| B | HOH551 |
| B | HOH560 |
| B | HOH601 |
| B | HOH604 |
| B | HOH617 |
| B | HOH658 |
| B | HOH689 |
| B | HOH691 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PPV C 401 |
| Chain | Residue |
| C | ARG108 |
| C | GLY109 |
| C | GLY227 |
| C | GLU228 |
| C | HOH513 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PPV D 401 |
| Chain | Residue |
| D | TYR107 |
| D | ARG108 |
| D | GLY109 |
| D | ALA226 |
| D | GLY227 |
| D | GLU228 |
| D | GLN275 |
| D | HOH517 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28283058, ECO:0007744|PDB:5ULJ |
| Chain | Residue | Details |
| A | TYR107 | |
| B | GLU179 | |
| B | GLU228 | |
| B | ASP230 | |
| B | GLU249 | |
| B | LEU250 | |
| B | LYS251 | |
| B | GLN275 | |
| C | TYR107 | |
| C | GLU179 | |
| C | GLU228 | |
| A | GLU179 | |
| C | ASP230 | |
| C | GLU249 | |
| C | LEU250 | |
| C | LYS251 | |
| C | GLN275 | |
| D | TYR107 | |
| D | GLU179 | |
| D | GLU228 | |
| D | ASP230 | |
| D | GLU249 | |
| A | GLU228 | |
| D | LEU250 | |
| D | LYS251 | |
| D | GLN275 | |
| A | ASP230 | |
| A | GLU249 | |
| A | LEU250 | |
| A | LYS251 | |
| A | GLN275 | |
| B | TYR107 |
