2G5F
The structure of MbtI from Mycobacterium Tuberculosis, the first enzyme in the synthesis of Mycobactin, reveals it to be a salicylate synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | L-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 | 0044847 | biological_process | iron acquisition from host |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000162 | biological_process | L-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 | 0044847 | biological_process | iron acquisition from host |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000162 | biological_process | L-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 | 0044847 | biological_process | iron acquisition from host |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000162 | biological_process | L-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 | 0044847 | biological_process | iron acquisition from host |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PYR A 2001 |
| Chain | Residue |
| A | ILE207 |
| A | TYR385 |
| A | LEU404 |
| A | ARG405 |
| A | GLY419 |
| A | ALA420 |
| A | LYS438 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR B 2002 |
| Chain | Residue |
| B | TYR385 |
| B | LEU404 |
| B | ARG405 |
| B | GLY419 |
| B | ALA420 |
| B | LYS438 |
| B | ILE207 |
| B | ALA362 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IMD A 3001 |
| Chain | Residue |
| A | ARG303 |
| A | GLU307 |
| D | GLU289 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD C 3002 |
| Chain | Residue |
| B | ARG303 |
| B | GLU307 |
| C | GLN123 |
| C | GLU289 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IMD C 3003 |
| Chain | Residue |
| B | GLU289 |
| C | ARG303 |
| C | GLU307 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IMD D 3004 |
| Chain | Residue |
| A | GLU289 |
| D | ARG303 |
| D | GLU307 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 4001 |
| Chain | Residue |
| C | LEU268 |
| C | THR271 |
| C | ARG405 |
| C | ALA418 |
| C | LYS438 |
| C | HOH4044 |
| C | HOH4108 |
| C | HOH4157 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 4002 |
| Chain | Residue |
| D | ARG405 |
| D | LYS438 |
| D | THR441 |
| D | HOH4069 |
| D | HOH4175 |
| D | HOH4187 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 4003 |
| Chain | Residue |
| A | ASP322 |
| A | THR325 |
| A | ARG327 |
| A | HIS334 |
| A | LEU335 |
| A | GLY336 |
| A | SER337 |
| A | THR338 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 4004 |
| Chain | Residue |
| B | ASP322 |
| B | THR325 |
| B | ARG327 |
| B | HIS334 |
| B | LEU335 |
| B | GLY336 |
| B | SER337 |
| B | THR338 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 4005 |
| Chain | Residue |
| C | GLU266 |
| C | ASP322 |
| C | THR325 |
| C | ARG327 |
| C | HIS334 |
| C | LEU335 |
| C | GLY336 |
| C | SER337 |
| C | THR338 |
| C | HOH4246 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 4006 |
| Chain | Residue |
| D | GLU266 |
| D | ASP322 |
| D | THR325 |
| D | ARG327 |
| D | HIS334 |
| D | LEU335 |
| D | GLY336 |
| D | SER337 |
| D | THR338 |
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 | |
| D | GLU297 | |
| D | GLU431 | |
| D | GLU434 | |
| A | GLU431 | |
| A | GLU434 | |
| B | GLU297 | |
| B | GLU431 | |
| B | GLU434 | |
| C | GLU297 | |
| C | GLU431 | |
| C | 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 |
| A | TYR385 | |
| C | ARG405 | |
| C | GLY419 | |
| C | LYS438 | |
| D | TYR385 | |
| D | ARG405 | |
| D | GLY419 | |
| D | LYS438 | |
| A | ARG405 | |
| A | GLY419 | |
| A | LYS438 | |
| B | TYR385 | |
| B | ARG405 | |
| B | GLY419 | |
| B | LYS438 | |
| C | TYR385 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1i7q |
| Chain | Residue | Details |
| A | HIS334 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1i7q |
| Chain | Residue | Details |
| B | HIS334 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1i7q |
| Chain | Residue | Details |
| C | HIS334 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1i7q |
| Chain | Residue | Details |
| D | HIS334 |
