4FQS
Crystal Structure of Mycobacterium tuberculosis ThyA in complex with UMP and Pemetrexed
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| A | 0032259 | biological_process | methylation |
| A | 0046079 | biological_process | dUMP catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| 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 | 0008168 | molecular_function | methyltransferase activity |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| B | 0032259 | biological_process | methylation |
| B | 0046079 | biological_process | dUMP catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UMP A 301 |
| Chain | Residue |
| A | ARG21 |
| A | ASN177 |
| A | HIS207 |
| A | TYR209 |
| A | LYA302 |
| A | HOH405 |
| A | HOH407 |
| B | ARG126 |
| B | ARG127 |
| A | TYR94 |
| A | CYS146 |
| A | HIS147 |
| A | GLN165 |
| A | ARG166 |
| A | SER167 |
| A | ALA168 |
| A | ASP169 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE LYA A 302 |
| Chain | Residue |
| A | GLU58 |
| A | ILE79 |
| A | TRP80 |
| A | TRP83 |
| A | LEU143 |
| A | ASP169 |
| A | LEU172 |
| A | GLY173 |
| A | PHE176 |
| A | VAL261 |
| A | ALA262 |
| A | UMP301 |
| A | HOH404 |
| A | HOH413 |
| A | HOH426 |
| A | HOH429 |
| A | HOH433 |
| A | HOH436 |
| A | HOH443 |
| A | HOH469 |
| A | HOH541 |
| A | HOH805 |
| A | HOH867 |
| A | HOH880 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UMP B 301 |
| Chain | Residue |
| A | ARG126 |
| A | ARG127 |
| B | ARG21 |
| B | TYR94 |
| B | CYS146 |
| B | HIS147 |
| B | GLN165 |
| B | ARG166 |
| B | SER167 |
| B | ALA168 |
| B | ASP169 |
| B | ASN177 |
| B | HIS207 |
| B | TYR209 |
| B | LYA302 |
| B | HOH411 |
| B | HOH430 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE LYA B 302 |
| Chain | Residue |
| B | GLU58 |
| B | ILE79 |
| B | TRP80 |
| B | TRP83 |
| B | LEU143 |
| B | ASP169 |
| B | LEU172 |
| B | GLY173 |
| B | PHE176 |
| B | TYR209 |
| B | VAL261 |
| B | ALA262 |
| B | UMP301 |
| B | HOH416 |
| B | HOH420 |
| B | HOH424 |
| B | HOH426 |
| B | HOH428 |
| B | HOH433 |
| B | HOH454 |
| B | HOH455 |
| B | HOH468 |
| B | HOH540 |
| B | HOH636 |
| B | HOH842 |
Functional Information from PROSITE/UniProt
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeierma.....LpPCHaffQFyV |
| Chain | Residue | Details |
| A | ARG126-VAL154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"3QJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FQS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"4FOG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"3QJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FQS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
