1DJ0
THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0001522 | biological_process | pseudouridine synthesis |
| A | 0003723 | molecular_function | RNA binding |
| A | 0008033 | biological_process | tRNA processing |
| A | 0009451 | biological_process | RNA modification |
| A | 0009982 | molecular_function | pseudouridine synthase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0031119 | biological_process | tRNA pseudouridine synthesis |
| A | 0034470 | biological_process | obsolete ncRNA processing |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0106029 | molecular_function | tRNA pseudouridine synthase activity |
| A | 0140098 | molecular_function | catalytic activity, acting on RNA |
| A | 0160147 | molecular_function | tRNA pseudouridine(38-40) synthase activity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0001522 | biological_process | pseudouridine synthesis |
| B | 0003723 | molecular_function | RNA binding |
| B | 0008033 | biological_process | tRNA processing |
| B | 0009451 | biological_process | RNA modification |
| B | 0009982 | molecular_function | pseudouridine synthase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0031119 | biological_process | tRNA pseudouridine synthesis |
| B | 0034470 | biological_process | obsolete ncRNA processing |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0106029 | molecular_function | tRNA pseudouridine synthase activity |
| B | 0140098 | molecular_function | catalytic activity, acting on RNA |
| B | 0160147 | molecular_function | tRNA pseudouridine(38-40) synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 600 |
| Chain | Residue |
| A | HIS202 |
| A | VAL204 |
| A | ARG205 |
| A | HOH741 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 601 |
| Chain | Residue |
| B | HIS202 |
| B | VAL204 |
| B | ARG205 |
| B | HOH658 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:10588695, ECO:0000269|PubMed:9425056 |
| Chain | Residue | Details |
| A | ASP60 | |
| B | ASP60 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17466622 |
| Chain | Residue | Details |
| A | TYR118 | |
| B | TYR118 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Interaction with tRNA; Important for base-flipping => ECO:0000269|PubMed:17466622 |
| Chain | Residue | Details |
| A | ARG58 | |
| B | ARG58 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Interaction with tRNA => ECO:0000269|PubMed:17466622 |
| Chain | Residue | Details |
| A | ARG78 | |
| A | ARG110 | |
| A | ARG126 | |
| A | PHE139 | |
| B | ARG78 | |
| B | ARG110 | |
| B | ARG126 | |
| B | PHE139 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11976723, 12581659, 20091078 |
| Chain | Residue | Details |
| A | ASP60 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11976723, 12581659, 20091078 |
| Chain | Residue | Details |
| B | ASP60 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 493 |
| Chain | Residue | Details |
| A | ARG58 | electrostatic stabiliser |
| A | ASP60 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ARG205 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 493 |
| Chain | Residue | Details |
| B | ARG58 | electrostatic stabiliser |
| B | ASP60 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ARG205 | electrostatic stabiliser |
