4F2V
Crystal Structure of de novo designed serine hydrolase, Northeast Structural Genomics Consortium (NESG) Target OR165
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003723 | molecular_function | RNA binding |
A | 0004799 | molecular_function | thymidylate synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006231 | biological_process | dTMP biosynthetic process |
A | 0006235 | biological_process | dTTP biosynthetic process |
A | 0006417 | biological_process | regulation of translation |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0009314 | biological_process | response to radiation |
A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
A | 0032259 | biological_process | methylation |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003723 | molecular_function | RNA binding |
B | 0004799 | molecular_function | thymidylate synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006231 | biological_process | dTMP biosynthetic process |
B | 0006235 | biological_process | dTTP biosynthetic process |
B | 0006417 | biological_process | regulation of translation |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0009165 | biological_process | nucleotide biosynthetic process |
B | 0009314 | biological_process | response to radiation |
B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
B | 0032259 | biological_process | methylation |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE LMU A 301 |
Chain | Residue |
A | ARG21 |
A | SER173 |
A | PHE176 |
A | GLY181 |
A | LEU184 |
A | PEG302 |
A | HOH415 |
A | HOH428 |
A | HOH461 |
B | ARG126 |
A | PHE62 |
A | TRP83 |
A | TRP98 |
A | ASN143 |
A | ALA144 |
A | SER146 |
A | ARG166 |
A | SER167 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEG A 302 |
Chain | Residue |
A | PHE62 |
A | HIS94 |
A | TRP98 |
A | PRO145 |
A | SER146 |
A | HIS147 |
A | LMU301 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE LMU B 301 |
Chain | Residue |
A | ARG126 |
B | PHE62 |
B | ILE79 |
B | LEU80 |
B | TRP83 |
B | ASN143 |
B | ALA144 |
B | SER146 |
B | ARG166 |
B | SER167 |
B | SER173 |
B | HOH443 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600 |
Chain | Residue | Details |
A | SER146 | |
B | SER146 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
Chain | Residue | Details |
A | ARG21 | |
A | ARG166 | |
A | ALA177 | |
A | HIS207 | |
B | ARG21 | |
B | ARG166 | |
B | ALA177 | |
B | HIS207 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS |
Chain | Residue | Details |
A | HIS51 | |
A | ASP169 | |
A | ALA263 | |
B | HIS51 | |
B | ASP169 | |
B | ALA263 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
Chain | Residue | Details |
A | ARG126 | |
B | ARG126 |