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 | 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 | 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 | 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 | 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 |