6GFG
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from A. thaliana in complex with D-chiro-IP6 and ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0030643 | biological_process | intracellular phosphate ion homeostasis |
| A | 0032942 | molecular_function | inositol tetrakisphosphate 2-kinase activity |
| A | 0032958 | biological_process | inositol phosphate biosynthetic process |
| A | 0035299 | molecular_function | inositol 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0030643 | biological_process | intracellular phosphate ion homeostasis |
| B | 0032942 | molecular_function | inositol tetrakisphosphate 2-kinase activity |
| B | 0032958 | biological_process | inositol phosphate biosynthetic process |
| B | 0035299 | molecular_function | inositol 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue KGN B 501 |
| Chain | Residue |
| A | ARG178 |
| B | ASN238 |
| B | ASP368 |
| B | TYR419 |
| B | GLY19 |
| B | GLY20 |
| B | ALA21 |
| B | ARG130 |
| B | LYS168 |
| B | LYS170 |
| B | ARG192 |
| B | LYS200 |
| site_id | AC2 |
| Number of Residues | 16 |
| 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 | LEU146 |
| B | ASN147 |
| B | ASP148 |
| B | HIS149 |
| B | GLU166 |
| B | MET372 |
| B | ASP407 |
| B | MG503 |
| B | MG504 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | ASP407 |
| B | ADP502 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 504 |
| Chain | Residue |
| B | ASP407 |
| B | ADP502 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 505 |
| Chain | Residue |
| B | HIS320 |
| B | CYS330 |
| B | CYS333 |
| B | HIS346 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue KGN A 501 |
| Chain | Residue |
| A | GLY19 |
| A | GLY20 |
| A | ARG130 |
| A | LYS168 |
| A | LYS170 |
| A | ARG192 |
| A | ASN238 |
| A | ASP368 |
| A | LYS411 |
| A | ARG415 |
| A | TYR419 |
| A | LEU422 |
| A | ADP502 |
| A | MG503 |
| A | MG504 |
| B | ARG178 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue ADP A 502 |
| Chain | Residue |
| A | GLU18 |
| A | GLY19 |
| A | GLY20 |
| A | ASN22 |
| A | ARG40 |
| A | ASN147 |
| A | ASP148 |
| A | HIS149 |
| A | GLU166 |
| A | ARG241 |
| A | ILE406 |
| A | ASP407 |
| A | KGN501 |
| A | MG503 |
| A | MG504 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | ASP407 |
| A | KGN501 |
| A | ADP502 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 504 |
| Chain | Residue |
| A | ASP368 |
| A | ASP407 |
| A | KGN501 |
| A | ADP502 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 505 |
| Chain | Residue |
| A | HIS320 |
| A | CYS330 |
| A | CYS333 |
| A | HIS346 |
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 |
| B | GLY19 | |
| A | ASP407 | |
| B | ARG40 | |
| B | ASN147 | |
| B | GLU166 | |
| B | ASP407 | |
| A | GLY19 | |
| A | ARG40 | |
| A | ASN147 | |
| A | 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 |
| B | ARG45 | |
| A | ARG45 | |
| A | ARG130 | |
| A | LYS170 | |
| A | LYS200 | |
| A | ASN238 | |
| A | ASP368 | |
| A | LYS411 | |
| A | ARG415 | |
| A | TYR419 | |
| B | ARG130 | |
| B | LYS170 | |
| B | LYS200 | |
| B | ASN238 | |
| B | ASP368 | |
| B | LYS411 | |
| B | ARG415 | |
| B | TYR419 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22745128 |
| Chain | Residue | Details |
| B | ARG241 | |
| A | 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 |
| B | HIS320 | |
| B | CYS330 | |
| B | HIS346 | |
| A | HIS320 | |
| A | CYS330 | |
| A | 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 |
| B | CYS333 | |
| A | CYS333 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| B | MET1 | |
| A | MET1 |
