3DL5
Crystal Structure of the A287F Active Site Mutant of TS-DHFR from Cryptosporidium hominis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| A | 0006231 | biological_process | dTMP biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| B | 0006231 | biological_process | dTMP biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| C | 0004146 | molecular_function | dihydrofolate reductase activity |
| C | 0004799 | molecular_function | thymidylate synthase activity |
| C | 0006231 | biological_process | dTMP biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| D | 0004146 | molecular_function | dihydrofolate reductase activity |
| D | 0004799 | molecular_function | thymidylate synthase activity |
| D | 0006231 | biological_process | dTMP biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| E | 0004146 | molecular_function | dihydrofolate reductase activity |
| E | 0004799 | molecular_function | thymidylate synthase activity |
| E | 0006231 | biological_process | dTMP biosynthetic process |
| E | 0006730 | biological_process | one-carbon metabolic process |
| E | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| E | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UMP A 603 |
| Chain | Residue |
| A | ARG257 |
| A | HIS464 |
| A | TYR466 |
| B | ARG382 |
| B | ARG383 |
| A | CYS402 |
| A | HIS403 |
| A | GLN422 |
| A | ARG423 |
| A | SER424 |
| A | CYS425 |
| A | ASP426 |
| A | ASN434 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CB3 A 604 |
| Chain | Residue |
| A | GLU294 |
| A | ILE315 |
| A | ASN319 |
| A | ASP426 |
| A | GLY430 |
| A | PHE433 |
| A | ASN434 |
| A | TYR466 |
| A | MET519 |
| A | ALA520 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DHF A 605 |
| Chain | Residue |
| A | ALA11 |
| A | LEU25 |
| A | ASP32 |
| A | LEU33 |
| A | PHE36 |
| A | SER37 |
| A | ARG70 |
| A | CYS113 |
| A | THR134 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NDP A 606 |
| Chain | Residue |
| A | ALA11 |
| A | ILE19 |
| A | GLY20 |
| A | ILE21 |
| A | GLY23 |
| A | GLN24 |
| A | LEU25 |
| A | GLY55 |
| A | ARG56 |
| A | LYS57 |
| A | THR58 |
| A | ILE75 |
| A | SER76 |
| A | SER77 |
| A | SER78 |
| A | ARG92 |
| A | GLY115 |
| A | GLU116 |
| A | SER117 |
| A | TYR119 |
| A | THR145 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UMP B 607 |
| Chain | Residue |
| A | ARG382 |
| A | ARG383 |
| B | ARG257 |
| B | CYS402 |
| B | HIS403 |
| B | GLN422 |
| B | ARG423 |
| B | SER424 |
| B | CYS425 |
| B | ASP426 |
| B | ASN434 |
| B | HIS464 |
| B | TYR466 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CB3 B 608 |
| Chain | Residue |
| B | PHE287 |
| B | SER290 |
| B | GLU294 |
| B | ILE315 |
| B | ASN319 |
| B | LEU399 |
| B | ASP426 |
| B | GLY430 |
| B | PHE433 |
| B | ASN434 |
| B | TYR466 |
| B | MET519 |
| B | ALA520 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DHF B 609 |
| Chain | Residue |
| B | ALA11 |
| B | LEU25 |
| B | ASP32 |
| B | LEU33 |
| B | PHE36 |
| B | SER37 |
| B | LEU67 |
| B | ARG70 |
| B | CYS113 |
| B | THR134 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NDP B 610 |
| Chain | Residue |
| B | ILE75 |
| B | SER76 |
| B | SER77 |
| B | SER78 |
| B | ARG92 |
| B | CYS113 |
| B | GLY115 |
| B | GLU116 |
| B | SER117 |
| B | TYR119 |
| B | THR145 |
| B | ALA11 |
| B | ILE19 |
| B | GLY20 |
| B | GLY23 |
| B | GLN24 |
| B | LEU25 |
| B | GLY55 |
| B | ARG56 |
| B | LYS57 |
| B | THR58 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UMP C 611 |
| Chain | Residue |
| C | ARG257 |
| C | CYS402 |
| C | HIS403 |
| C | GLN422 |
| C | ARG423 |
| C | SER424 |
| C | CYS425 |
| C | ASP426 |
| C | ASN434 |
| C | HIS464 |
| C | TYR466 |
| D | ARG382 |
| D | ARG383 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CB3 C 612 |
| Chain | Residue |
| C | PHE287 |
| C | SER290 |
| C | GLU294 |
| C | ILE315 |
| C | ASN319 |
| C | ASP426 |
| C | LEU429 |
| C | GLY430 |
| C | PHE433 |
| C | ASN434 |
| C | TYR466 |
| C | MET519 |
| C | ALA520 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DHF C 613 |
| Chain | Residue |
| C | ASP32 |
| C | LEU33 |
| C | PHE36 |
| C | SER37 |
| C | LEU67 |
| C | ARG70 |
| C | CYS113 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP C 614 |
| Chain | Residue |
| C | ALA11 |
| C | ILE19 |
| C | GLY55 |
| C | ARG56 |
| C | LYS57 |
| C | THR58 |
| C | ILE75 |
| C | SER76 |
| C | SER77 |
| C | ARG92 |
| C | ASN93 |
| C | CYS113 |
| C | GLY114 |
| C | GLY115 |
| C | GLU116 |
| C | SER117 |
| C | ILE118 |
| C | TYR119 |
| C | THR145 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UMP D 615 |
| Chain | Residue |
| C | ARG382 |
| C | ARG383 |
| D | ARG257 |
| D | CYS402 |
| D | HIS403 |
| D | GLN422 |
| D | ARG423 |
| D | SER424 |
| D | CYS425 |
| D | ASP426 |
| D | GLY430 |
| D | ASN434 |
| D | HIS464 |
| D | TYR466 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CB3 D 616 |
| Chain | Residue |
| D | ILE315 |
| D | ASP426 |
| D | LEU429 |
| D | GLY430 |
| D | PHE433 |
| D | ASN434 |
| D | TYR466 |
| D | MET519 |
| D | ALA520 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DHF D 617 |
| Chain | Residue |
| D | ALA11 |
| D | LEU25 |
| D | ASP32 |
| D | LEU33 |
| D | PHE36 |
| D | SER37 |
| D | THR58 |
| D | ILE62 |
| D | LEU67 |
| D | ARG70 |
| D | CYS113 |
| D | THR134 |
| site_id | BC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP D 618 |
| Chain | Residue |
| D | ALA11 |
| D | ILE19 |
| D | GLY23 |
| D | GLN24 |
| D | GLY55 |
| D | ARG56 |
| D | LYS57 |
| D | THR58 |
| D | ILE75 |
| D | SER76 |
| D | SER77 |
| D | SER78 |
| D | ARG92 |
| D | CYS113 |
| D | GLY115 |
| D | GLU116 |
| D | SER117 |
| D | TYR119 |
| D | THR145 |
| site_id | BC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UMP E 619 |
| Chain | Residue |
| E | ARG257 |
| E | ARG382 |
| E | ARG383 |
| E | CYS402 |
| E | HIS403 |
| E | GLN422 |
| E | ARG423 |
| E | SER424 |
| E | CYS425 |
| E | ASP426 |
| E | ASN434 |
| E | HIS464 |
| E | TYR466 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CB3 E 620 |
| Chain | Residue |
| E | GLU294 |
| E | ASP426 |
| E | LEU429 |
| E | GLY430 |
| E | PHE433 |
| E | ASN434 |
| E | TYR466 |
| E | MET519 |
| E | ALA520 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DHF E 621 |
| Chain | Residue |
| E | ALA11 |
| E | ASP32 |
| E | LEU33 |
| E | PHE36 |
| E | SER37 |
| E | LEU67 |
| E | ARG70 |
| E | CYS113 |
| E | THR134 |
| site_id | CC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NDP E 622 |
| Chain | Residue |
| E | ALA11 |
| E | ILE19 |
| E | GLY23 |
| E | GLN24 |
| E | GLY55 |
| E | ARG56 |
| E | LYS57 |
| E | THR58 |
| E | ILE75 |
| E | SER76 |
| E | SER77 |
| E | SER78 |
| E | ARG92 |
| E | CYS113 |
| E | GLY114 |
| E | GLY115 |
| E | GLU116 |
| E | SER117 |
| E | ILE118 |
| E | TYR119 |
| E | ASP121 |
| E | THR145 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGingqLPWsise.DlkfFskiT |
| Chain | Residue | Details |
| A | GLY18-THR40 |
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrhIltaWNpsalsqma.....LpPCHvlsQYyV |
| Chain | Residue | Details |
| A | ARG382-VAL410 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| A | LEU25 | |
| A | ASP32 |
| site_id | CSA10 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| E | ASP426 | |
| E | ASP462 | |
| E | GLU294 | |
| E | HIS464 | |
| E | SER424 | |
| E | CYS402 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| B | LEU25 | |
| B | ASP32 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| C | LEU25 | |
| C | ASP32 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| D | LEU25 | |
| D | ASP32 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| E | LEU25 | |
| E | ASP32 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| A | ASP426 | |
| A | ASP462 | |
| A | GLU294 | |
| A | HIS464 | |
| A | SER424 | |
| A | CYS402 |
| site_id | CSA7 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| B | ASP426 | |
| B | ASP462 | |
| B | GLU294 | |
| B | HIS464 | |
| B | SER424 | |
| B | CYS402 |
| site_id | CSA8 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| C | ASP426 | |
| C | ASP462 | |
| C | GLU294 | |
| C | HIS464 | |
| C | SER424 | |
| C | CYS402 |
| site_id | CSA9 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| D | ASP426 | |
| D | ASP462 | |
| D | GLU294 | |
| D | HIS464 | |
| D | SER424 | |
| D | CYS402 |
