2BLE
Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003920 | molecular_function | GMP reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0006163 | biological_process | purine nucleotide metabolic process |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009409 | biological_process | response to cold |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902560 | cellular_component | GMP reductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A1345 |
| Chain | Residue |
| A | THR57 |
| A | SER246 |
| A | GLY247 |
| A | HOH2102 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A1346 |
| Chain | Residue |
| A | SER105 |
| A | GLU140 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 5GP A1344 |
| Chain | Residue |
| A | SER184 |
| A | CYS186 |
| A | ASP219 |
| A | GLY220 |
| A | GLY221 |
| A | MET240 |
| A | LEU241 |
| A | GLY242 |
| A | GLY243 |
| A | GLY268 |
| A | MET269 |
| A | SER270 |
| A | SER271 |
| A | ARG286 |
| A | ALA287 |
| A | SER288 |
| A | GLY290 |
| A | HOH2077 |
| A | HOH2078 |
| A | HOH2082 |
| A | HOH2100 |
| A | HOH2124 |
| A | HOH2125 |
| A | HOH2126 |
| A | ALA53 |
| A | MET55 |
| A | GLY183 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGVGpGSVCtT |
| Chain | Residue | Details |
| A | ILE176-THR188 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
