4KPW
Crystal structure of His-tagged human thymidylate synthase R175A mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000900 | molecular_function | mRNA regulatory element binding translation repressor activity |
A | 0004799 | molecular_function | thymidylate synthase activity |
A | 0005542 | molecular_function | folic acid binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005829 | cellular_component | cytosol |
A | 0006231 | biological_process | dTMP biosynthetic process |
A | 0006235 | biological_process | dTTP biosynthetic process |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
A | 0017148 | biological_process | negative regulation of translation |
A | 0032259 | biological_process | methylation |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
A | 0046653 | biological_process | tetrahydrofolate metabolic process |
A | 0071897 | biological_process | DNA biosynthetic process |
A | 1990825 | molecular_function | sequence-specific mRNA binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | ARG50 |
A | ARG78 |
A | ARG176 |
A | ARG185 |
A | PRO305 |
A | THR306 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | ARG215 |
A | SER216 |
A | ASN183 |
A | HIS196 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | GLU272 |
A | ARG274 |
A | HIS304 |
A | HOH550 |
A | HOH583 |
A | HOH609 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 404 |
Chain | Residue |
A | GLY29 |
A | ARG64 |
A | TYR65 |
A | SER66 |
A | GLU70 |
A | PHE276 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 405 |
Chain | Residue |
A | GLN36 |
A | GLN62 |
A | ALA63 |
A | VAL223 |
A | HIS250 |
A | LEU252 |
A | HOH502 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 406 |
Chain | Residue |
A | GLY217 |
A | ASP218 |
A | GLY222 |
A | ASN226 |
A | HOH524 |
Functional Information from PROSITE/UniProt
site_id | PS00091 |
Number of Residues | 28 |
Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RiiMca.WNprdlplma.....LpPCHalcQFyV |
Chain | Residue | Details |
A | ARG176-VAL203 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |