2A7R
Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)
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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046037 | biological_process | GMP metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902560 | cellular_component | GMP reductase complex |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003920 | molecular_function | GMP reductase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0006163 | biological_process | purine nucleotide metabolic process |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046037 | biological_process | GMP metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1902560 | cellular_component | GMP reductase complex |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003920 | molecular_function | GMP reductase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006144 | biological_process | purine nucleobase metabolic process |
| C | 0006163 | biological_process | purine nucleotide metabolic process |
| C | 0009117 | biological_process | nucleotide metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046037 | biological_process | GMP metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1902560 | cellular_component | GMP reductase complex |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003920 | molecular_function | GMP reductase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006144 | biological_process | purine nucleobase metabolic process |
| D | 0006163 | biological_process | purine nucleotide metabolic process |
| D | 0009117 | biological_process | nucleotide metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046037 | biological_process | GMP metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1902560 | cellular_component | GMP reductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | THR33 |
| A | ARG34 |
| A | SER35 |
| A | LYS325 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | PHE149 |
| A | PRO150 |
| A | GLN151 |
| A | HIS152 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1400 |
| Chain | Residue |
| B | ARG34 |
| B | SER35 |
| B | LYS323 |
| B | LYS325 |
| B | THR33 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1401 |
| Chain | Residue |
| B | PHE149 |
| B | PRO150 |
| B | GLN151 |
| B | HIS152 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2400 |
| Chain | Residue |
| C | THR33 |
| C | ARG34 |
| C | SER35 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2401 |
| Chain | Residue |
| C | PHE149 |
| C | PRO150 |
| C | GLN151 |
| C | HIS152 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3400 |
| Chain | Residue |
| D | THR33 |
| D | ARG34 |
| D | SER35 |
| D | LYS325 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3500 |
| Chain | Residue |
| D | GLY183 |
| D | SER184 |
| D | GLY220 |
| D | GLY221 |
| D | CYS222 |
| D | GLY242 |
| D | GLY243 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 5GP A 500 |
| Chain | Residue |
| A | MET55 |
| A | GLY183 |
| A | SER184 |
| A | CYS186 |
| A | THR188 |
| A | ASP219 |
| A | GLY220 |
| A | GLY221 |
| A | GLY242 |
| A | GLY243 |
| A | GLY268 |
| A | MET269 |
| A | SER270 |
| A | ARG286 |
| A | ALA287 |
| A | SER288 |
| A | GLY290 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 5GP B 500 |
| Chain | Residue |
| B | ALA53 |
| B | MET55 |
| B | GLY183 |
| B | SER184 |
| B | CYS186 |
| B | THR188 |
| B | ASP219 |
| B | GLY220 |
| B | GLY221 |
| B | GLY242 |
| B | GLY243 |
| B | GLY268 |
| B | SER270 |
| B | ARG286 |
| B | SER288 |
| B | GLY290 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 5GP C 500 |
| Chain | Residue |
| C | ALA53 |
| C | MET55 |
| C | SER184 |
| C | CYS186 |
| C | THR188 |
| C | ASP219 |
| C | GLY220 |
| C | GLY221 |
| C | GLY242 |
| C | GLY243 |
| C | GLY268 |
| C | MET269 |
| C | SER270 |
| C | GLY290 |
Functional Information from PROSITE/UniProt
| site_id | PS00487 |
| Number of Residues | 13 |
| Details | IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSVCtT |
| Chain | Residue | Details |
| A | ILE176-THR188 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22037469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22037469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 38 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03195","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






