1I9A
STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050992 | biological_process | dimethylallyl diphosphate biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004452 | molecular_function | isopentenyl-diphosphate delta-isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008299 | biological_process | isoprenoid 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 1001 |
| Chain | Residue |
| A | HIS25 |
| A | HIS32 |
| A | HIS69 |
| A | GLU114 |
| A | GLU116 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 2001 |
| Chain | Residue |
| B | GLU1116 |
| B | HIS1025 |
| B | HIS1032 |
| B | HIS1069 |
| B | GLU1114 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12630859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15643873","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Essential for catalytic activity"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details |
| Chain | Residue | Details |
| A | TRP161 | |
| A | GLU87 | |
| A | GLU116 | |
| A | CYS67 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue | Details |
| B | TRP1161 | |
| B | CYS1067 | |
| B | GLU1087 | |
| B | GLU1116 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 190 |
| Chain | Residue | Details |
| A | THR29 | metal ligand |
| A | SER36 | metal ligand |
| A | GLN71 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY73 | metal ligand |
| A | GLU91 | metal ligand |
| A | ASP108 | hydrogen bond acceptor, hydrogen bond donor, proton donor |
| A | CYS118 | metal ligand |
| A | VAL120 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
| A | ARG169 | electrostatic stabiliser, polar/non-polar interaction |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 190 |
| Chain | Residue | Details |
| B | THR1029 | metal ligand |
| B | SER1036 | metal ligand |
| B | GLN1071 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY1073 | metal ligand |
| B | GLU1091 | metal ligand |
| B | ASP1108 | hydrogen bond acceptor, hydrogen bond donor, proton donor |
| B | CYS1118 | metal ligand |
| B | VAL1120 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
| B | ARG1169 | electrostatic stabiliser, polar/non-polar interaction |
