5EX4
3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis complexed with tryptophan in all three allosteric binding sites
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003849 | molecular_function | 3-deoxy-7-phosphoheptulonate synthase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051260 | biological_process | protein homooligomerization |
B | 0003849 | molecular_function | 3-deoxy-7-phosphoheptulonate synthase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030145 | molecular_function | manganese ion binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MN A 501 |
Chain | Residue |
A | CYS87 |
A | HIS369 |
A | GLU411 |
A | ASP441 |
A | HOH740 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue TRP A 502 |
Chain | Residue |
A | CYS231 |
A | ASN237 |
A | LEU238 |
A | THR240 |
A | HOH631 |
A | HOH635 |
A | HOH705 |
A | HOH833 |
A | VAL111 |
A | LYS123 |
A | ALA192 |
A | LEU194 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | ARG135 |
A | ASP138 |
A | ARG145 |
A | ARG148 |
A | HIS164 |
A | HOH612 |
A | HOH627 |
A | HOH768 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue TRP A 504 |
Chain | Residue |
A | PHE91 |
A | ARG171 |
A | ALA174 |
A | ASN175 |
A | ALA178 |
A | GOL507 |
A | HOH660 |
B | ILE7 |
B | TYR173 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | GLU63 |
A | THR187 |
A | ALA241 |
A | GLU242 |
A | ILE243 |
A | HOH841 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue PO4 A 506 |
Chain | Residue |
A | GLY282 |
A | GLU283 |
A | LYS306 |
A | ARG337 |
A | HIS369 |
A | HOH725 |
A | HOH757 |
A | HOH800 |
A | HOH829 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | ILE7 |
A | VAL170 |
A | TRP504 |
B | ILE7 |
B | TRP503 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 501 |
Chain | Residue |
B | ARG135 |
B | SER136 |
B | ALA137 |
B | ARG284 |
B | HOH601 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue MN B 502 |
Chain | Residue |
B | CYS87 |
B | HIS369 |
B | GLU411 |
B | ASP441 |
B | HOH735 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue TRP B 503 |
Chain | Residue |
A | ASP10 |
A | VAL170 |
A | TYR173 |
A | GOL507 |
B | PHE91 |
B | ARG171 |
B | ALA174 |
B | ASN175 |
B | ALA178 |
B | HOH667 |
site_id | AD2 |
Number of Residues | 12 |
Details | binding site for residue TRP B 504 |
Chain | Residue |
B | VAL111 |
B | LYS123 |
B | ALA192 |
B | LEU194 |
B | CYS231 |
B | ASN237 |
B | LEU238 |
B | THR240 |
B | HOH623 |
B | HOH703 |
B | HOH705 |
B | HOH818 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
A | THR24 |
A | ASP27 |
A | HOH671 |
A | HOH775 |
B | ARG25 |
B | VAL298 |
B | HOH675 |
B | HOH720 |
B | HOH799 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | ALA241 |
B | GLU242 |
B | ILE243 |
B | GLU63 |
B | ARG66 |
B | MET180 |
B | THR187 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue PO4 B 507 |
Chain | Residue |
B | GLY282 |
B | GLU283 |
B | LYS306 |
B | ARG337 |
B | HIS369 |
B | HOH777 |
B | HOH782 |
B | HOH787 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue TRP B 508 |
Chain | Residue |
B | LEU15 |
B | PRO16 |
B | LEU18 |
B | ARG23 |
B | LEU26 |
B | GLU53 |
B | ARG256 |
B | LEU259 |
B | ARG260 |
B | HOH622 |
B | HOH750 |
B | HOH791 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue CL B 509 |
Chain | Residue |
B | LEU18 |
B | ARG23 |
B | HOH845 |
B | HOH893 |
site_id | AD8 |
Number of Residues | 8 |
Details | binding site for residue GOL B 510 |
Chain | Residue |
B | GLN70 |
B | VAL121 |
B | GLU242 |
B | HOH623 |
B | HOH671 |
B | HOH691 |
B | HOH773 |
B | HOH818 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16288916, ECO:0007744|PDB:2B7O |
Chain | Residue | Details |
A | CYS87 | |
B | ARG126 | |
B | GLU283 | |
B | LYS306 | |
B | ARG337 | |
B | HIS369 | |
B | GLU411 | |
B | ASP441 | |
A | ARG126 | |
A | GLU283 | |
A | LYS306 | |
A | ARG337 | |
A | HIS369 | |
A | GLU411 | |
A | ASP441 | |
B | CYS87 |