6PBJ
The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase with Gly190Pro mutation
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 | 8 |
Details | binding site for residue PO4 A 501 |
Chain | Residue |
A | GLY282 |
A | GLU283 |
A | LYS306 |
A | ARG337 |
A | HIS369 |
A | HOH721 |
A | HOH741 |
A | HOH796 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | PRO61 |
A | SER62 |
A | HOH633 |
A | HOH711 |
A | HOH743 |
B | ARG100 |
B | PRO190 |
A | VAL60 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | ALA35 |
A | GLN36 |
A | HOH635 |
B | SER136 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | THR39 |
A | ARG145 |
A | ARG148 |
A | HIS164 |
A | HOH602 |
A | HOH604 |
A | HOH638 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MN A 505 |
Chain | Residue |
A | CYS87 |
A | HIS369 |
A | GLU411 |
A | ASP441 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL A 506 |
Chain | Residue |
A | HIS341 |
A | ARG386 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue CL A 507 |
Chain | Residue |
A | HIS326 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue CL A 508 |
Chain | Residue |
A | ARG171 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue PEG A 509 |
Chain | Residue |
A | GLU63 |
A | ARG184 |
A | THR187 |
A | ILE243 |
A | HOH678 |
A | HOH766 |
A | HOH805 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue PG4 A 510 |
Chain | Residue |
A | ILE7 |
A | ARG171 |
A | ALA174 |
A | ASN175 |
B | VAL55 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue PO4 B 501 |
Chain | Residue |
B | GLY282 |
B | GLU283 |
B | LYS306 |
B | ARG337 |
B | HIS369 |
B | HOH663 |
B | HOH729 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | ARG23 |
B | ARG256 |
B | HOH658 |
B | HOH702 |
B | HOH715 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
A | ARG100 |
A | HOH634 |
B | VAL60 |
B | PRO61 |
B | SER62 |
B | HOH621 |
B | HOH772 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 504 |
Chain | Residue |
B | ARG135 |
B | SER136 |
B | ALA137 |
B | ARG284 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue MN B 505 |
Chain | Residue |
B | CYS87 |
B | HIS369 |
B | GLU411 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue CL B 506 |
Chain | Residue |
B | ARG49 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue CL B 507 |
Chain | Residue |
B | HIS326 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue CL B 508 |
Chain | Residue |
B | GLY339 |
B | HIS341 |
B | ARG386 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue PEG B 509 |
Chain | Residue |
A | ARG145 |
B | ALA34 |
B | ALA35 |
B | GLN36 |
B | HOH775 |
site_id | AE2 |
Number of Residues | 8 |
Details | binding site for residue PEG B 510 |
Chain | Residue |
A | PRO61 |
A | ARG260 |
A | LEU261 |
A | LEU274 |
A | HOH626 |
B | GLU96 |
B | ARG100 |
B | HOH688 |
site_id | AE3 |
Number of Residues | 7 |
Details | binding site for residue PEG B 511 |
Chain | Residue |
B | GLU63 |
B | MET180 |
B | THR187 |
B | ILE243 |
B | HOH606 |
B | HOH617 |
B | HOH731 |
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 | GLU411 | |
A | ASP441 | |
B | CYS87 | |
B | ARG126 | |
B | GLU283 | |
B | LYS306 | |
B | ARG337 | |
B | HIS369 | |
B | GLU411 | |
B | ASP441 | |
A | CYS87 | |
A | ARG126 | |
A | GLU283 | |
A | LYS306 | |
A | ARG337 | |
A | HIS369 |