3VEH
Structure of a M. tuberculosis salicylate synthase, MbtI, in complex with an inhibitor methylAMT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | tryptophan biosynthetic process |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004106 | molecular_function | chorismate mutase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008909 | molecular_function | isochorismate synthase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009697 | biological_process | salicylic acid biosynthetic process |
| A | 0010106 | biological_process | cellular response to iron ion starvation |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
| A | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052572 | biological_process | response to host immune response |
| B | 0000162 | biological_process | tryptophan biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004106 | molecular_function | chorismate mutase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008909 | molecular_function | isochorismate synthase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009697 | biological_process | salicylic acid biosynthetic process |
| B | 0010106 | biological_process | cellular response to iron ion starvation |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016833 | molecular_function | oxo-acid-lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
| B | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052572 | biological_process | response to host immune response |
| C | 0000162 | biological_process | tryptophan biosynthetic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004106 | molecular_function | chorismate mutase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008909 | molecular_function | isochorismate synthase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009697 | biological_process | salicylic acid biosynthetic process |
| C | 0010106 | biological_process | cellular response to iron ion starvation |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016833 | molecular_function | oxo-acid-lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
| C | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0052572 | biological_process | response to host immune response |
| D | 0000162 | biological_process | tryptophan biosynthetic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004106 | molecular_function | chorismate mutase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008909 | molecular_function | isochorismate synthase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009697 | biological_process | salicylic acid biosynthetic process |
| D | 0010106 | biological_process | cellular response to iron ion starvation |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016833 | molecular_function | oxo-acid-lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019540 | biological_process | catechol-containing siderophore biosynthetic process |
| D | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0052572 | biological_process | response to host immune response |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 0GA A 501 |
| Chain | Residue |
| A | PRO251 |
| A | HOH722 |
| A | HOH749 |
| A | HOH775 |
| A | THR271 |
| A | HIS334 |
| A | THR361 |
| A | TYR385 |
| A | ALA418 |
| A | GLY419 |
| A | LYS438 |
| A | HOH610 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SCN A 502 |
| Chain | Residue |
| A | THR232 |
| A | PRO233 |
| A | TYR249 |
| A | SER250 |
| A | PRO251 |
| A | ARG329 |
| A | GLY330 |
| A | ARG405 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | ASP104 |
| A | GLN105 |
| A | ALA394 |
| A | ASP395 |
| A | HOH626 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 0GA B 501 |
| Chain | Residue |
| B | PRO251 |
| B | ALA269 |
| B | GLY270 |
| B | THR271 |
| B | HIS334 |
| B | THR361 |
| B | TYR385 |
| B | LEU404 |
| B | ALA418 |
| B | GLY419 |
| B | LYS438 |
| B | HOH605 |
| B | HOH753 |
| B | HOH812 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SCN B 502 |
| Chain | Residue |
| B | ASN231 |
| B | THR232 |
| B | PRO233 |
| B | TYR249 |
| B | ARG329 |
| B | GLY330 |
| B | ARG405 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | GLU70 |
| B | ARG81 |
| B | GLN83 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 504 |
| Chain | Residue |
| A | ARG156 |
| A | HOH826 |
| B | THR38 |
| B | GLU43 |
| B | GLN240 |
| B | HOH703 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 0GA C 501 |
| Chain | Residue |
| C | THR271 |
| C | HIS334 |
| C | THR361 |
| C | TYR385 |
| C | ALA418 |
| C | GLY419 |
| C | LYS438 |
| C | HOH614 |
| C | HOH695 |
| C | HOH717 |
| C | HOH725 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SCN C 502 |
| Chain | Residue |
| C | ASN231 |
| C | THR232 |
| C | PRO233 |
| C | TYR249 |
| C | ARG329 |
| C | GLY330 |
| C | ARG405 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PEG C 503 |
| Chain | Residue |
| C | ARG138 |
| C | THR139 |
| C | ASP152 |
| C | GLY154 |
| C | HIS157 |
| C | HOH636 |
| C | HOH658 |
| C | HOH808 |
| C | HOH851 |
| D | GLU39 |
| D | SER40 |
| D | ASP42 |
| D | ARG156 |
| D | HOH609 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 504 |
| Chain | Residue |
| C | VAL214 |
| C | PHE216 |
| C | GLY412 |
| C | THR414 |
| C | HOH679 |
| C | HOH785 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG C 505 |
| Chain | Residue |
| C | ILE244 |
| C | ARG382 |
| C | LEU384 |
| C | TYR385 |
| C | TRP415 |
| C | HOH841 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 506 |
| Chain | Residue |
| C | ARG158 |
| C | HOH712 |
| C | HOH816 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 0GA D 501 |
| Chain | Residue |
| D | THR271 |
| D | HIS334 |
| D | THR361 |
| D | TYR385 |
| D | ALA418 |
| D | GLY419 |
| D | LYS438 |
| D | HOH629 |
| D | HOH725 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K D 502 |
| Chain | Residue |
| D | ALA34 |
| D | ALA35 |
| D | THR38 |
| D | GLU39 |
| D | HOH635 |
| D | HOH643 |
| D | HOH652 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9X9I8 |
| Chain | Residue | Details |
| A | GLU252 | |
| B | GLU252 | |
| C | GLU252 | |
| D | GLU252 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697 |
| Chain | Residue | Details |
| A | GLY270 | |
| B | GLY270 | |
| C | GLY270 | |
| D | GLY270 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20512795 |
| Chain | Residue | Details |
| A | GLU297 | |
| A | GLU431 | |
| A | GLU434 | |
| B | GLU297 | |
| B | GLU431 | |
| B | GLU434 | |
| C | GLU297 | |
| C | GLU431 | |
| C | GLU434 | |
| D | GLU297 | |
| D | GLU431 | |
| D | GLU434 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697 |
| Chain | Residue | Details |
| B | TYR385 | |
| B | ARG405 | |
| B | GLY419 | |
| B | LYS438 | |
| C | TYR385 | |
| C | ARG405 | |
| C | GLY419 | |
| C | LYS438 | |
| D | TYR385 | |
| D | ARG405 | |
| D | GLY419 | |
| D | LYS438 | |
| A | TYR385 | |
| A | ARG405 | |
| A | GLY419 | |
| A | LYS438 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl => ECO:0000269|PubMed:17240979 |
| Chain | Residue | Details |
| A | LEU268 | |
| B | LEU268 | |
| C | LEU268 | |
| D | LEU268 |
