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 |