4GIM
Crystal Structure of Pseudouridine Monophosphate Glycosidase Complexed with Pseudouridine 5'-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001522 | biological_process | pseudouridine synthesis |
| A | 0004730 | molecular_function | pseudouridylate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046113 | biological_process | nucleobase catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0001522 | biological_process | pseudouridine synthesis |
| B | 0004730 | molecular_function | pseudouridylate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046113 | biological_process | nucleobase catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0001522 | biological_process | pseudouridine synthesis |
| C | 0004730 | molecular_function | pseudouridylate synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046113 | biological_process | nucleobase catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE PSU A 400 |
| Chain | Residue |
| A | GLU31 |
| A | ASP149 |
| A | LEU274 |
| A | HOH505 |
| A | HOH507 |
| A | HOH508 |
| A | HOH511 |
| A | HOH516 |
| A | HOH519 |
| A | HOH532 |
| A | HOH553 |
| A | THR33 |
| A | HOH555 |
| A | HOH558 |
| A | HOH571 |
| A | HOH573 |
| C | HOH505 |
| A | ILE34 |
| A | GLY38 |
| A | LYS93 |
| A | THR112 |
| A | VAL113 |
| A | GLY132 |
| A | SER147 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | ASP145 |
| A | HOH502 |
| A | HOH503 |
| A | HOH516 |
| C | HOH502 |
| C | HOH505 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PSU B 400 |
| Chain | Residue |
| B | GLU31 |
| B | THR33 |
| B | ILE34 |
| B | GLY38 |
| B | LYS93 |
| B | THR112 |
| B | VAL113 |
| B | GLY132 |
| B | SER147 |
| B | ASP149 |
| B | PHE196 |
| B | LEU274 |
| B | HOH503 |
| B | HOH505 |
| B | HOH507 |
| B | HOH509 |
| B | HOH510 |
| B | HOH513 |
| B | HOH516 |
| B | HOH517 |
| B | HOH541 |
| B | HOH606 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 401 |
| Chain | Residue |
| A | HOH504 |
| B | ASP145 |
| B | HOH501 |
| B | HOH503 |
| B | HOH506 |
| B | HOH513 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE PSU C 400 |
| Chain | Residue |
| B | HOH526 |
| C | GLU31 |
| C | THR33 |
| C | ILE34 |
| C | GLY38 |
| C | LYS93 |
| C | THR112 |
| C | VAL113 |
| C | GLY132 |
| C | SER147 |
| C | ASP149 |
| C | PHE196 |
| C | LEU274 |
| C | HOH508 |
| C | HOH511 |
| C | HOH515 |
| C | HOH537 |
| C | HOH538 |
| C | HOH554 |
| C | HOH556 |
| C | HOH571 |
| C | HOH577 |
| C | HOH589 |
| C | HOH590 |
| C | HOH631 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 401 |
| Chain | Residue |
| B | HOH502 |
| B | HOH526 |
| C | ASP145 |
| C | HOH507 |
| C | HOH511 |
| C | HOH528 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23066817","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23066817","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23066817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
