4Q0E
Crystal structure of TS-DHFR from Cryptosporidium hominis in complex with NADPH, FdUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-L-glutamic acid.
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 | 21 |
Details | BINDING SITE FOR RESIDUE NDP A 601 |
Chain | Residue |
A | VAL10 |
A | THR58 |
A | ILE75 |
A | SER76 |
A | SER77 |
A | SER78 |
A | ARG92 |
A | GLY114 |
A | GLY115 |
A | GLU116 |
A | SER117 |
A | ALA11 |
A | THR145 |
A | 2XB604 |
A | ILE19 |
A | GLY23 |
A | GLN24 |
A | LEU25 |
A | GLY55 |
A | ARG56 |
A | LYS57 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UFP A 602 |
Chain | Residue |
A | ARG257 |
A | TYR342 |
A | CYS402 |
A | HIS403 |
A | ARG423 |
A | SER424 |
A | CYS425 |
A | ASP426 |
A | GLY430 |
A | ASN434 |
A | HIS464 |
A | TYR466 |
A | 2XB603 |
A | HOH704 |
C | ARG382 |
C | ARG383 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB A 603 |
Chain | Residue |
A | SER290 |
A | ILE315 |
A | ASN319 |
A | ASP426 |
A | LEU429 |
A | GLY430 |
A | PHE433 |
A | TYR466 |
A | MET519 |
A | ALA520 |
A | UFP602 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB A 604 |
Chain | Residue |
A | VAL9 |
A | VAL10 |
A | ALA11 |
A | ASP32 |
A | LYS34 |
A | PHE36 |
A | SER37 |
A | ARG70 |
A | CYS113 |
A | THR134 |
A | NDP601 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NDP B 601 |
Chain | Residue |
B | VAL10 |
B | ALA11 |
B | ILE19 |
B | GLY23 |
B | GLN24 |
B | LEU25 |
B | GLY55 |
B | ARG56 |
B | LYS57 |
B | THR58 |
B | ILE75 |
B | SER76 |
B | SER77 |
B | SER78 |
B | ARG92 |
B | GLY114 |
B | GLY115 |
B | GLU116 |
B | SER117 |
B | THR145 |
B | 2XB604 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UFP B 602 |
Chain | Residue |
B | ARG257 |
B | TYR342 |
B | CYS402 |
B | HIS403 |
B | ARG423 |
B | SER424 |
B | CYS425 |
B | ASP426 |
B | GLY430 |
B | ASN434 |
B | HIS464 |
B | TYR466 |
B | 2XB603 |
D | ARG382 |
D | ARG383 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB B 603 |
Chain | Residue |
B | LEU429 |
B | GLY430 |
B | PHE433 |
B | TYR466 |
B | MET519 |
B | ALA520 |
B | UFP602 |
B | SER290 |
B | ILE315 |
B | ASN319 |
B | ASP426 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB B 604 |
Chain | Residue |
B | VAL9 |
B | VAL10 |
B | ALA11 |
B | ASP32 |
B | LYS34 |
B | PHE36 |
B | SER37 |
B | ARG70 |
B | CYS113 |
B | THR134 |
B | NDP601 |
site_id | AC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NDP C 601 |
Chain | Residue |
C | VAL10 |
C | ALA11 |
C | ILE19 |
C | GLY23 |
C | GLN24 |
C | LEU25 |
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 | THR145 |
C | 2XB604 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE UFP C 602 |
Chain | Residue |
A | ARG382 |
A | ARG383 |
C | ARG257 |
C | TYR342 |
C | CYS402 |
C | HIS403 |
C | ARG423 |
C | SER424 |
C | CYS425 |
C | ASP426 |
C | ASN434 |
C | HIS464 |
C | TYR466 |
C | 2XB603 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB C 603 |
Chain | Residue |
C | SER290 |
C | ILE315 |
C | ASN319 |
C | ASP426 |
C | LEU429 |
C | GLY430 |
C | PHE433 |
C | TYR466 |
C | MET519 |
C | ALA520 |
C | UFP602 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 2XB C 604 |
Chain | Residue |
C | VAL9 |
C | VAL10 |
C | ALA11 |
C | LEU25 |
C | ASP32 |
C | LYS34 |
C | PHE36 |
C | SER37 |
C | ARG70 |
C | CYS113 |
C | THR134 |
C | NDP601 |
site_id | BC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NDP D 601 |
Chain | Residue |
D | VAL10 |
D | ALA11 |
D | ILE19 |
D | GLY23 |
D | GLN24 |
D | LEU25 |
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 | THR145 |
D | 2XB604 |
site_id | BC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UFP D 602 |
Chain | Residue |
B | ARG382 |
B | ARG383 |
D | ARG257 |
D | TYR342 |
D | CYS402 |
D | HIS403 |
D | ARG423 |
D | SER424 |
D | CYS425 |
D | ASP426 |
D | GLY430 |
D | ASN434 |
D | HIS464 |
D | TYR466 |
D | 2XB603 |
site_id | BC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB D 603 |
Chain | Residue |
D | SER290 |
D | ILE315 |
D | ASN319 |
D | ASP426 |
D | LEU429 |
D | GLY430 |
D | PHE433 |
D | TYR466 |
D | MET519 |
D | ALA520 |
D | UFP602 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB D 604 |
Chain | Residue |
D | VAL9 |
D | VAL10 |
D | ALA11 |
D | ASP32 |
D | LYS34 |
D | PHE36 |
D | SER37 |
D | ARG70 |
D | CYS113 |
D | THR134 |
D | NDP601 |
site_id | BC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NDP E 601 |
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 | GLY114 |
E | GLY115 |
E | GLU116 |
E | SER117 |
E | THR145 |
E | 2XB604 |
site_id | BC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE UFP E 602 |
Chain | Residue |
E | ARG257 |
E | TYR342 |
E | CYS402 |
E | HIS403 |
E | ARG423 |
E | SER424 |
E | CYS425 |
E | ASP426 |
E | GLY430 |
E | ASN434 |
E | HIS464 |
E | TYR466 |
E | 2XB603 |
site_id | CC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB E 603 |
Chain | Residue |
E | SER290 |
E | ILE315 |
E | ASN319 |
E | ASP426 |
E | LEU429 |
E | GLY430 |
E | PHE433 |
E | TYR466 |
E | MET519 |
E | ALA520 |
E | UFP602 |
site_id | CC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 2XB E 604 |
Chain | Residue |
E | VAL9 |
E | VAL10 |
E | ALA11 |
E | ASP32 |
E | LYS34 |
E | PHE36 |
E | SER37 |
E | ARG70 |
E | CYS113 |
E | THR134 |
E | NDP601 |
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 |