5CKV
DAHP synthase from Mycobacterium tuberculosis, fully inhibited by tyrosine, phenylalanine, and tryptophan
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 | 1 |
Details | binding site for residue CL A 501 |
Chain | Residue |
A | ALA141 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | ARG135 |
A | SER136 |
A | ARG284 |
A | LYS380 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | ASP138 |
A | ARG145 |
A | ARG148 |
A | HIS164 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | GLY282 |
A | GLU283 |
A | ARG284 |
A | LYS306 |
A | ARG337 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | GLN70 |
A | VAL121 |
A | VAL122 |
A | GLU242 |
A | TRP507 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | GLU63 |
A | ARG184 |
A | THR187 |
A | GLU242 |
A | ILE243 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue TRP A 507 |
Chain | Residue |
A | VAL111 |
A | LYS123 |
A | ALA192 |
A | ASN237 |
A | THR240 |
A | GOL505 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue MN A 508 |
Chain | Residue |
A | CYS87 |
A | HIS369 |
A | GLU411 |
A | ASP441 |
A | HOH604 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue PHE A 509 |
Chain | Residue |
A | PHE91 |
A | ARG171 |
A | ALA174 |
A | ASN175 |
B | VAL5 |
B | VAL55 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CL B 501 |
Chain | Residue |
B | LEU18 |
B | ARG23 |
B | ALA159 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue MN B 502 |
Chain | Residue |
B | CYS87 |
B | HIS369 |
B | GLU411 |
B | ASP441 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
B | GLY282 |
B | GLU283 |
B | ARG284 |
B | LYS306 |
B | ARG337 |
B | HIS369 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 504 |
Chain | Residue |
B | ARG135 |
B | SER136 |
B | ALA137 |
B | ARG284 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
A | GLN36 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | LEU30 |
B | ALA34 |
B | ASP253 |
B | ARG256 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 507 |
Chain | Residue |
A | ASP27 |
A | ALA28 |
B | ARG25 |
B | GLN297 |
B | VAL298 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue TYR B 508 |
Chain | Residue |
B | PRO16 |
B | LEU18 |
B | ARG23 |
B | GLU53 |
B | ARG256 |
site_id | AD9 |
Number of Residues | 9 |
Details | binding site for residue TRP B 509 |
Chain | Residue |
B | VAL111 |
B | LYS123 |
B | ALA192 |
B | CYS231 |
B | ASN237 |
B | LEU238 |
B | THR240 |
B | ALA241 |
B | HOH606 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue PHE B 510 |
Chain | Residue |
A | ILE9 |
A | TYR173 |
B | PHE91 |
B | ARG171 |
B | ASN175 |
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 |