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 | 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 | 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 | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008 |
Chain | Residue | Details |
A | PHE149 | |
B | PHE149 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000269|Ref.8, ECO:0007744|PDB:3QJ7, ECO:0007744|PDB:4FOX, ECO:0007744|PDB:4FQS |
Chain | Residue | Details |
A | THR24 | |
A | ASP169 | |
A | SER180 | |
A | ASP210 | |
B | THR24 | |
B | ASP169 | |
B | SER180 | |
B | ASP210 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:4FOG |
Chain | Residue | Details |
A | SER54 | |
A | LEU172 | |
A | ALA262 | |
B | SER54 | |
B | LEU172 | |
B | ALA262 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:3QJ7, ECO:0007744|PDB:4FOX, ECO:0007744|PDB:4FQS |
Chain | Residue | Details |
A | ILE129 | |
B | ILE129 |