2I6K
Crystal structure of human type I IPP isomerase complexed with a substrate analog
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006695 | biological_process | cholesterol biosynthetic process |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0009240 | biological_process | isopentenyl diphosphate biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050992 | biological_process | dimethylallyl diphosphate biosynthetic process |
| B | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0006695 | biological_process | cholesterol biosynthetic process |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0009240 | biological_process | isopentenyl diphosphate biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050992 | biological_process | dimethylallyl diphosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 228 |
| Chain | Residue |
| A | HIS40 |
| A | HIS51 |
| A | HIS88 |
| A | GLU146 |
| A | GLU148 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | HOH515 |
| A | HOH541 |
| A | CYS86 |
| A | SER87 |
| A | GLU115 |
| A | EA2401 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 303 |
| Chain | Residue |
| A | GLU97 |
| A | SER99 |
| A | HOH521 |
| A | HOH556 |
| A | HOH557 |
| B | HOH552 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE EA2 A 401 |
| Chain | Residue |
| A | LYS36 |
| A | ARG70 |
| A | LYS74 |
| A | CYS86 |
| A | SER87 |
| A | HIS88 |
| A | ARG111 |
| A | GLU115 |
| A | TYR136 |
| A | GLU146 |
| A | GLU148 |
| A | MG302 |
| A | HOH515 |
| A | HOH541 |
| A | HOH548 |
| A | HOH549 |
| A | HOH567 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 501 |
| Chain | Residue |
| A | ASP28 |
| A | GLU98 |
| A | ARG133 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY A 502 |
| Chain | Residue |
| A | GLU26 |
| A | ASN27 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 503 |
| Chain | Residue |
| A | LEU183 |
| A | ALA186 |
| A | ALA187 |
| A | LYS198 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 228 |
| Chain | Residue |
| B | HIS40 |
| B | HIS51 |
| B | HIS88 |
| B | GLU146 |
| B | GLU148 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | CYS86 |
| B | SER87 |
| B | GLU115 |
| B | EA2402 |
| B | HOH508 |
| B | HOH549 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 304 |
| Chain | Residue |
| B | GLU97 |
| B | SER99 |
| B | HOH558 |
| B | HOH559 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE EA2 B 402 |
| Chain | Residue |
| B | LYS36 |
| B | ARG70 |
| B | LYS74 |
| B | CYS86 |
| B | SER87 |
| B | HIS88 |
| B | ARG111 |
| B | GLU115 |
| B | TYR136 |
| B | GLU146 |
| B | GLU148 |
| B | MG301 |
| B | HOH508 |
| B | HOH517 |
| B | HOH549 |
| B | HOH564 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY B 504 |
| Chain | Residue |
| A | ARG110 |
| B | LYS30 |
| B | ILE31 |
| B | HOH518 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | CYS86 | |
| A | GLU148 | |
| B | CYS86 | |
| B | GLU148 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17250851 |
| Chain | Residue | Details |
| A | LYS36 | |
| A | ARG70 | |
| A | LYS74 | |
| A | SER87 | |
| B | LYS36 | |
| B | ARG70 | |
| B | LYS74 | |
| B | SER87 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS40 | |
| A | HIS51 | |
| A | GLU146 | |
| A | GLU148 | |
| B | HIS40 | |
| B | HIS51 | |
| B | GLU146 | |
| B | GLU148 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS176 | |
| B | LYS176 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1i9a |
| Chain | Residue | Details |
| A | GLU148 | |
| A | CYS86 | |
| A | GLU115 | |
| A | TRP196 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1i9a |
| Chain | Residue | Details |
| B | GLU148 | |
| B | CYS86 | |
| B | GLU115 | |
| B | TRP196 |
