3DL6
Crystal Structure of the A287F/S290G 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 | 11 |
Details | BINDING SITE FOR RESIDUE CB3 A 604 |
Chain | Residue |
A | GLU294 |
A | ILE315 |
A | ASN319 |
A | ASP426 |
A | LEU429 |
A | GLY430 |
A | PHE433 |
A | ASN434 |
A | TYR466 |
A | MET519 |
A | ALA520 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DHF A 605 |
Chain | Residue |
A | ASP32 |
A | LEU33 |
A | PHE36 |
A | SER37 |
A | ILE62 |
A | LEU67 |
A | ARG70 |
A | CYS113 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NDP A 606 |
Chain | Residue |
A | ALA11 |
A | ILE19 |
A | GLY23 |
A | GLN24 |
A | LEU25 |
A | GLY55 |
A | ARG56 |
A | LYS57 |
A | THR58 |
A | ILE75 |
A | SER76 |
A | SER77 |
A | ARG92 |
A | GLY114 |
A | GLY115 |
A | GLU116 |
A | SER117 |
A | ILE118 |
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 | 12 |
Details | BINDING SITE FOR RESIDUE CB3 B 608 |
Chain | Residue |
B | PHE287 |
B | ILE315 |
B | TRP316 |
B | ASN319 |
B | LEU399 |
B | ASP426 |
B | LEU429 |
B | GLY430 |
B | PHE433 |
B | TYR466 |
B | MET519 |
B | ALA520 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE DHF B 609 |
Chain | Residue |
B | ALA11 |
B | LEU25 |
B | ASP32 |
B | LEU33 |
B | PHE36 |
B | SER37 |
B | ILE62 |
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 | SER77 |
B | SER78 |
B | ARG92 |
B | GLY114 |
B | GLY115 |
B | GLU116 |
B | SER117 |
B | ILE118 |
B | TYR119 |
B | THR145 |
B | ALA11 |
B | ILE19 |
B | GLY20 |
B | GLY23 |
B | GLN24 |
B | GLY55 |
B | ARG56 |
B | LYS57 |
B | THR58 |
B | ILE75 |
B | SER76 |
site_id | AC9 |
Number of Residues | 14 |
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 | GLY430 |
C | ASN434 |
C | HIS464 |
C | TYR466 |
D | ARG382 |
D | ARG383 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CB3 C 612 |
Chain | Residue |
C | PHE287 |
C | GLU294 |
C | ILE315 |
C | TRP316 |
C | ASN319 |
C | ASP426 |
C | LEU429 |
C | GLY430 |
C | PHE433 |
C | TYR466 |
C | MET519 |
C | ALA520 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DHF C 613 |
Chain | Residue |
C | ASP32 |
C | LEU33 |
C | PHE36 |
C | SER37 |
C | ILE62 |
C | LEU67 |
C | ARG70 |
C | CYS113 |
site_id | BC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NDP C 614 |
Chain | Residue |
C | ALA11 |
C | ILE19 |
C | GLY20 |
C | GLY23 |
C | GLN24 |
C | GLY55 |
C | ARG56 |
C | LYS57 |
C | THR58 |
C | ILE75 |
C | SER76 |
C | SER77 |
C | SER78 |
C | ARG92 |
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 | 11 |
Details | BINDING SITE FOR RESIDUE CB3 D 616 |
Chain | Residue |
D | PHE287 |
D | GLU294 |
D | ILE315 |
D | ASN319 |
D | ASP426 |
D | LEU429 |
D | GLY430 |
D | PHE433 |
D | TYR466 |
D | MET519 |
D | ALA520 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DHF D 617 |
Chain | Residue |
D | ALA11 |
D | ASP32 |
D | LEU33 |
D | PHE36 |
D | SER37 |
D | ILE62 |
D | LEU67 |
D | ARG70 |
site_id | BC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NDP D 618 |
Chain | Residue |
D | ALA11 |
D | ILE19 |
D | GLY23 |
D | GLY55 |
D | ARG56 |
D | LYS57 |
D | THR58 |
D | ILE75 |
D | SER76 |
D | SER77 |
D | SER78 |
D | ARG92 |
D | GLY114 |
D | GLY115 |
D | GLU116 |
D | SER117 |
D | ILE118 |
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 | 12 |
Details | BINDING SITE FOR RESIDUE CB3 E 620 |
Chain | Residue |
E | PHE287 |
E | GLU294 |
E | ILE315 |
E | ASN319 |
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 | ILE62 |
E | LEU67 |
E | ARG70 |
E | CYS113 |
site_id | CC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NDP E 622 |
Chain | Residue |
E | ALA11 |
E | ILE19 |
E | GLY20 |
E | ILE21 |
E | GLY23 |
E | GLN24 |
E | GLY55 |
E | ARG56 |
E | LYS57 |
E | THR58 |
E | ILE75 |
E | SER76 |
E | SER77 |
E | SER78 |
E | ARG92 |
E | ASN93 |
E | GLY115 |
E | GLU116 |
E | SER117 |
E | ILE118 |
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 |