2GQ2
Mycobacterium tuberculosis ThyX-NADP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| 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 | 0032259 | biological_process | methylation |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| 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 | 0032259 | biological_process | methylation |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0004799 | molecular_function | thymidylate synthase activity |
| C | 0006231 | biological_process | dTMP biosynthetic process |
| C | 0006235 | biological_process | dTTP biosynthetic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0004799 | molecular_function | thymidylate synthase activity |
| D | 0006231 | biological_process | dTMP biosynthetic process |
| D | 0006235 | biological_process | dTTP biosynthetic process |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0009165 | biological_process | nucleotide biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0032259 | biological_process | methylation |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 501 |
| Chain | Residue |
| A | ARG115 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD A 502 |
| Chain | Residue |
| A | ARG87 |
| D | ARG87 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD D 503 |
| Chain | Residue |
| A | ASN177 |
| D | ARG87 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD D 505 |
| Chain | Residue |
| D | THR239 |
| D | GLU240 |
| D | GOL408 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD D 507 |
| Chain | Residue |
| D | VAL206 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD C 509 |
| Chain | Residue |
| B | ASN177 |
| C | ARG87 |
| C | GLN106 |
| C | ARG172 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD B 510 |
| Chain | Residue |
| B | ARG87 |
| B | ARG172 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD C 511 |
| Chain | Residue |
| B | HIS98 |
| C | HIS98 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD D 512 |
| Chain | Residue |
| A | HIS98 |
| A | HOH800 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD C 513 |
| Chain | Residue |
| B | HOH690 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD D 514 |
| Chain | Residue |
| A | ASP205 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD A 515 |
| Chain | Residue |
| A | GLY121 |
| A | VAL206 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K C 601 |
| Chain | Residue |
| A | NAP300 |
| B | NAP300 |
| B | HOH628 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K D 602 |
| Chain | Residue |
| A | NAP300 |
| B | NAP300 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 603 |
| Chain | Residue |
| C | NAP300 |
| D | NAP300 |
| D | HOH687 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K B 604 |
| Chain | Residue |
| C | HOH610 |
| D | NAP300 |
| site_id | BC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP A 300 |
| Chain | Residue |
| A | TYR101 |
| A | SER102 |
| A | GLN103 |
| A | SER105 |
| A | HOH779 |
| A | HOH787 |
| A | HOH800 |
| A | HOH806 |
| B | NAP300 |
| C | SER71 |
| C | GLU74 |
| C | HIS98 |
| C | ASN188 |
| C | ARG190 |
| C | HIS194 |
| C | K601 |
| D | ARG95 |
| D | HIS96 |
| D | ARG97 |
| D | HIS98 |
| D | HIS194 |
| D | ARG199 |
| D | K602 |
| site_id | BC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP B 300 |
| Chain | Residue |
| A | NAP300 |
| A | HOH779 |
| A | HOH806 |
| B | GLN103 |
| B | SER105 |
| B | HOH628 |
| B | HOH683 |
| C | ARG95 |
| C | HIS96 |
| C | ARG97 |
| C | HIS194 |
| C | ARG199 |
| C | K601 |
| D | SER71 |
| D | GLU74 |
| D | HIS98 |
| D | ASN188 |
| D | ARG190 |
| D | HIS194 |
| D | K602 |
| D | HOH634 |
| D | HOH676 |
| site_id | CC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP C 300 |
| Chain | Residue |
| C | HOH683 |
| C | HOH684 |
| D | NAP300 |
| D | HOH642 |
| A | SER71 |
| A | GLU74 |
| A | HIS98 |
| A | ASN188 |
| A | ARG190 |
| A | HIS194 |
| A | K603 |
| A | PGE701 |
| A | HOH785 |
| B | ARG95 |
| B | HIS96 |
| B | ARG97 |
| B | HIS194 |
| B | ARG199 |
| C | TYR101 |
| C | SER102 |
| C | GLN103 |
| C | SER105 |
| C | HOH610 |
| C | HOH620 |
| C | HOH635 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGE A 701 |
| Chain | Residue |
| A | TYR44 |
| A | GLY68 |
| A | HIS69 |
| A | PHE70 |
| A | SER71 |
| A | HOH810 |
| C | SER105 |
| C | NAP300 |
| site_id | CC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP D 300 |
| Chain | Residue |
| A | ARG95 |
| A | HIS96 |
| A | ARG97 |
| A | HIS98 |
| A | HIS194 |
| A | ARG199 |
| A | K603 |
| B | SER71 |
| B | GLU74 |
| B | HIS98 |
| B | ASN188 |
| B | ARG190 |
| B | HIS194 |
| B | K604 |
| B | HOH611 |
| B | HOH680 |
| C | NAP300 |
| C | HOH635 |
| D | TYR101 |
| D | SER102 |
| D | GLN103 |
| D | SER105 |
| D | HOH624 |
| D | HOH642 |
| D | HOH687 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 401 |
| Chain | Residue |
| A | LYS14 |
| A | THR15 |
| A | GLY32 |
| A | SER77 |
| A | TYR189 |
| A | VAL222 |
| A | HOH766 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| B | LYS14 |
| B | THR15 |
| B | GLY31 |
| B | GLY32 |
| B | VAL78 |
| B | TYR189 |
| B | VAL222 |
| B | HOH674 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| C | LYS14 |
| C | THR15 |
| C | GLY32 |
| C | SER77 |
| C | TYR189 |
| C | VAL222 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 404 |
| Chain | Residue |
| D | LYS14 |
| D | THR15 |
| D | GLY32 |
| D | SER77 |
| D | VAL78 |
| D | TYR189 |
| D | VAL222 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 405 |
| Chain | Residue |
| B | TYR81 |
| B | ARG182 |
| D | ASP22 |
| D | VAL23 |
| D | PRO24 |
| D | GLN45 |
| D | TRP47 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 407 |
| Chain | Residue |
| C | ILE213 |
| C | GLU240 |
| C | HOH658 |
| C | HOH659 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 408 |
| Chain | Residue |
| D | ARG210 |
| D | THR239 |
| D | GLU240 |
| D | IOD505 |
| D | HOH640 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Involved in ionization of N3 of dUMP, leading to its activation => ECO:0000255|HAMAP-Rule:MF_01408 |
| Chain | Residue | Details |
| A | ARG199 | |
| B | ARG199 | |
| C | ARG199 | |
| D | ARG199 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16139296, ECO:0007744|PDB:2AF6, ECO:0007744|PDB:3GWC, ECO:0007744|PDB:3HZG |
| Chain | Residue | Details |
| A | SER71 | |
| B | HIS194 | |
| C | SER71 | |
| C | ARG95 | |
| C | GLN103 | |
| C | ASN188 | |
| C | HIS194 | |
| D | SER71 | |
| D | ARG95 | |
| D | GLN103 | |
| D | ASN188 | |
| A | ARG95 | |
| D | HIS194 | |
| A | GLN103 | |
| A | ASN188 | |
| A | HIS194 | |
| B | SER71 | |
| B | ARG95 | |
| B | GLN103 | |
| B | ASN188 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:16139296, ECO:0007744|PDB:2AF6 |
| Chain | Residue | Details |
| A | ARG87 | |
| A | ARG172 | |
| B | ARG87 | |
| B | ARG172 | |
| C | ARG87 | |
| C | ARG172 | |
| D | ARG87 | |
| D | ARG172 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16139296, ECO:0007744|PDB:2AF6 |
| Chain | Residue | Details |
| A | GLU92 | |
| A | ARG199 | |
| B | GLU92 | |
| B | ARG199 | |
| C | GLU92 | |
| C | ARG199 | |
| D | GLU92 | |
| D | ARG199 |
