2B7O
The Structure of 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate Synthase from Mycobacterium tuberculosis
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 | 4 |
Details | BINDING SITE FOR RESIDUE MN A 700 |
Chain | Residue |
A | CYS87 |
A | HIS369 |
A | GLU411 |
A | ASP441 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
Chain | Residue |
A | ARG135 |
A | SER136 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
Chain | Residue |
B | ARG284 |
B | PRO134 |
B | ARG135 |
B | SER136 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN B 701 |
Chain | Residue |
B | CYS87 |
B | HIS369 |
B | GLU411 |
B | ASP441 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PEP A 702 |
Chain | Residue |
A | ARG126 |
A | GLU248 |
A | TRP280 |
A | GLY282 |
A | GLU283 |
A | ARG284 |
A | LYS306 |
A | ARG337 |
A | HIS369 |
A | HOH2115 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CE1 A 1001 |
Chain | Residue |
A | PHE91 |
A | MSE92 |
A | ASN94 |
A | ARG171 |
A | ALA174 |
A | ASN175 |
B | LEU12 |
B | SER54 |
B | ASN175 |
B | HOH2088 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PEP B 703 |
Chain | Residue |
B | ARG126 |
B | GLU248 |
B | TRP280 |
B | GLY282 |
B | GLU283 |
B | LYS306 |
B | ARG337 |
B | HIS369 |
B | GLU411 |
B | HOH2030 |
B | HOH2031 |
B | HOH2034 |
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 |