6FL8
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from A. thaliana in complex with purpurogallin and ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0010264 | biological_process | myo-inositol hexakisphosphate biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0030643 | biological_process | intracellular phosphate ion homeostasis |
A | 0032942 | molecular_function | inositol-1,4,5,6-tetrakisphosphate 2-kinase activity |
A | 0035299 | molecular_function | inositol-1,3,4,5,6-pentakisphosphate 2-kinase activity |
A | 0042742 | biological_process | defense response to bacterium |
A | 0046872 | molecular_function | metal ion binding |
A | 0048527 | biological_process | lateral root development |
A | 0050832 | biological_process | defense response to fungus |
A | 0051607 | biological_process | defense response to virus |
A | 0055062 | biological_process | phosphate ion homeostasis |
A | 0102731 | molecular_function | inositol-1,3,4,6-tetrakisphosphate 2-kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0010264 | biological_process | myo-inositol hexakisphosphate biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0030643 | biological_process | intracellular phosphate ion homeostasis |
B | 0032942 | molecular_function | inositol-1,4,5,6-tetrakisphosphate 2-kinase activity |
B | 0035299 | molecular_function | inositol-1,3,4,5,6-pentakisphosphate 2-kinase activity |
B | 0042742 | biological_process | defense response to bacterium |
B | 0046872 | molecular_function | metal ion binding |
B | 0048527 | biological_process | lateral root development |
B | 0050832 | biological_process | defense response to fungus |
B | 0051607 | biological_process | defense response to virus |
B | 0055062 | biological_process | phosphate ion homeostasis |
B | 0102731 | molecular_function | inositol-1,3,4,6-tetrakisphosphate 2-kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue TIY A 501 |
Chain | Residue |
A | GLY20 |
A | HOH683 |
A | HOH697 |
A | ARG130 |
A | LYS168 |
A | LYS170 |
A | LYS200 |
A | ASN238 |
A | ASP368 |
A | EDO505 |
A | HOH614 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue ADP A 502 |
Chain | Residue |
A | ARG16 |
A | GLY19 |
A | GLY20 |
A | ALA21 |
A | ASN22 |
A | VAL24 |
A | ARG40 |
A | ASN147 |
A | ASP148 |
A | HIS149 |
A | GLU166 |
A | ARG241 |
A | MET372 |
A | ASP407 |
A | MG503 |
A | HOH638 |
A | HOH673 |
A | HOH698 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | ASP407 |
A | ADP502 |
A | HOH697 |
A | HOH698 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN A 504 |
Chain | Residue |
A | HIS320 |
A | CYS330 |
A | CYS333 |
A | HIS346 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LYS200 |
A | ASN238 |
A | TIY501 |
A | HOH617 |
B | ARG178 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | CYS171 |
A | PRO175 |
A | ASP311 |
A | ASP314 |
A | HOH607 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue TIY B 501 |
Chain | Residue |
B | LYS168 |
B | LYS170 |
B | ARG192 |
B | HIS196 |
B | LYS200 |
B | ASN238 |
B | ASP368 |
B | TYR419 |
B | EDO510 |
B | HOH686 |
site_id | AC8 |
Number of Residues | 19 |
Details | binding site for residue ADP B 502 |
Chain | Residue |
B | ARG16 |
B | GLY19 |
B | GLY20 |
B | ALA21 |
B | ASN22 |
B | VAL24 |
B | ARG40 |
B | ASN147 |
B | ASP148 |
B | HIS149 |
B | GLU166 |
B | ARG241 |
B | MET372 |
B | ASP407 |
B | MG503 |
B | MG504 |
B | HOH648 |
B | HOH654 |
B | HOH672 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue MG B 503 |
Chain | Residue |
B | ASP407 |
B | SER409 |
B | ADP502 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG B 504 |
Chain | Residue |
B | ASP407 |
B | ADP502 |
B | HOH647 |
B | HOH654 |
B | HOH672 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN B 505 |
Chain | Residue |
B | HIS320 |
B | CYS330 |
B | CYS333 |
B | HIS346 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue TRS B 506 |
Chain | Residue |
A | ASN73 |
A | ILE76 |
B | ASP324 |
B | HIS346 |
B | LEU348 |
B | LEU350 |
B | SER353 |
B | HOH602 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | ASP314 |
B | HOH624 |
B | HOH643 |
B | CYS171 |
B | PRO175 |
B | ASP311 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue EDO B 508 |
Chain | Residue |
B | TYR266 |
B | ASP270 |
B | ASP280 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue EDO B 509 |
Chain | Residue |
A | ILE204 |
B | ARG178 |
B | PHE179 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 510 |
Chain | Residue |
B | LYS200 |
B | GLU205 |
B | ASN238 |
B | TIY501 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:20453199, ECO:0000305|PubMed:22745128 |
Chain | Residue | Details |
A | GLY19 | |
B | ASP407 | |
A | ARG40 | |
A | ASN147 | |
A | GLU166 | |
A | ASP407 | |
B | GLY19 | |
B | ARG40 | |
B | ASN147 | |
B | GLU166 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000305|PubMed:20453199, ECO:0000305|PubMed:22362712, ECO:0000305|PubMed:22684075, ECO:0000305|PubMed:22745128 |
Chain | Residue | Details |
A | ARG45 | |
B | ARG45 | |
B | ARG130 | |
B | LYS170 | |
B | LYS200 | |
B | ASN238 | |
B | ASP368 | |
B | LYS411 | |
B | ARG415 | |
B | TYR419 | |
A | ARG130 | |
A | LYS170 | |
A | LYS200 | |
A | ASN238 | |
A | ASP368 | |
A | LYS411 | |
A | ARG415 | |
A | TYR419 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22745128 |
Chain | Residue | Details |
A | ARG241 | |
B | ARG241 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0007744|PDB:2XAL, ECO:0007744|PDB:2XAM, ECO:0007744|PDB:2XAN, ECO:0007744|PDB:2XAO, ECO:0007744|PDB:2XAR, ECO:0007744|PDB:3UDT, ECO:0007744|PDB:3UDZ, ECO:0007744|PDB:4AQK, ECO:0007744|PDB:4AXC, ECO:0007744|PDB:4AXD, ECO:0007744|PDB:4AXE, ECO:0007744|PDB:4AXF, ECO:0007744|PDB:4LV7 |
Chain | Residue | Details |
A | HIS320 | |
A | CYS330 | |
A | HIS346 | |
B | HIS320 | |
B | CYS330 | |
B | HIS346 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:2XAL, ECO:0007744|PDB:2XAM, ECO:0007744|PDB:2XAN, ECO:0007744|PDB:2XAO, ECO:0007744|PDB:2XAR, ECO:0007744|PDB:3UDT, ECO:0007744|PDB:4AQK, ECO:0007744|PDB:4AXC, ECO:0007744|PDB:4AXD, ECO:0007744|PDB:4AXE, ECO:0007744|PDB:4AXF, ECO:0007744|PDB:4LV7 |
Chain | Residue | Details |
A | CYS333 | |
B | CYS333 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |