3AU9
Crystal structure of the quaternary complex-1 of an isomerase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0009536 | cellular_component | plastid |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0020011 | cellular_component | apicoplast |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0009536 | cellular_component | plastid |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0020011 | cellular_component | apicoplast |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 501 |
| Chain | Residue |
| A | GLY84 |
| A | SER117 |
| A | HIS136 |
| A | GLY180 |
| A | ILE181 |
| A | ASP182 |
| A | GLN185 |
| A | ALA203 |
| A | ASN204 |
| A | LYS205 |
| A | GLU206 |
| A | THR86 |
| A | ASP231 |
| A | MET298 |
| A | GLY299 |
| A | ILE302 |
| A | MET360 |
| A | FOM701 |
| A | HOH765 |
| A | HOH777 |
| A | HOH790 |
| A | HOH851 |
| A | GLY87 |
| A | HOH891 |
| A | HOH1103 |
| A | HOH1149 |
| A | SER88 |
| A | ILE89 |
| A | TYR113 |
| A | VAL114 |
| A | ASN115 |
| A | LYS116 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | LYS205 |
| A | ASP231 |
| A | GLU233 |
| A | GLU315 |
| A | FOM701 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FOM A 701 |
| Chain | Residue |
| A | LYS205 |
| A | ASP231 |
| A | SER232 |
| A | GLU233 |
| A | SER269 |
| A | SER270 |
| A | HIS293 |
| A | TRP296 |
| A | MET298 |
| A | SER306 |
| A | ASN311 |
| A | LYS312 |
| A | GLU315 |
| A | NDP501 |
| A | MG601 |
| A | HOH922 |
| A | HOH927 |
| A | HOH987 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP B 502 |
| Chain | Residue |
| B | GLY84 |
| B | THR86 |
| B | GLY87 |
| B | SER88 |
| B | ILE89 |
| B | TYR113 |
| B | VAL114 |
| B | ASN115 |
| B | LYS116 |
| B | SER117 |
| B | HIS136 |
| B | GLY180 |
| B | ILE181 |
| B | ASP182 |
| B | GLN185 |
| B | ALA203 |
| B | ASN204 |
| B | LYS205 |
| B | GLU206 |
| B | ASP231 |
| B | MET298 |
| B | GLY299 |
| B | ILE302 |
| B | MET360 |
| B | FOM702 |
| B | HOH707 |
| B | HOH735 |
| B | HOH739 |
| B | HOH753 |
| B | HOH757 |
| B | HOH760 |
| B | HOH848 |
| B | HOH1003 |
| B | HOH1144 |
| B | HOH1147 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | LYS205 |
| B | ASP231 |
| B | GLU233 |
| B | GLU315 |
| B | FOM702 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FOM B 702 |
| Chain | Residue |
| B | SER269 |
| B | SER270 |
| B | HIS293 |
| B | TRP296 |
| B | MET298 |
| B | ILE302 |
| B | ASN311 |
| B | LYS312 |
| B | GLU315 |
| B | NDP502 |
| B | MG602 |
| B | HOH754 |
| B | HOH888 |
| B | HOH919 |
| B | LYS205 |
| B | ASP231 |
| B | SER232 |
| B | GLU233 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 489 |
| Chain | Residue |
| A | ASP242 |
| A | HOH903 |
| B | GLN239 |
| B | LEU241 |
| B | HOH721 |
| B | HOH762 |
| B | HOH843 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 490 |
| Chain | Residue |
| B | ASN452 |
| B | HOH775 |
| B | HOH876 |
| B | HOH883 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22355528, ECO:0007744|PDB:3AU8, ECO:0007744|PDB:3AU9, ECO:0007744|PDB:3AUA |
| Chain | Residue | Details |
| A | THR86 | |
| A | ASN115 | |
| B | THR86 | |
| B | ASN115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P45568 |
| Chain | Residue | Details |
| A | LYS205 | |
| B | SER270 | |
| B | HIS293 | |
| B | SER306 | |
| B | ASN311 | |
| B | LYS312 | |
| A | SER232 | |
| A | SER270 | |
| A | HIS293 | |
| A | SER306 | |
| A | ASN311 | |
| A | LYS312 | |
| B | LYS205 | |
| B | SER232 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22355528, ECO:0007744|PDB:3AU9, ECO:0007744|PDB:3AUA |
| Chain | Residue | Details |
| A | GLU206 | |
| A | GLY299 | |
| B | GLU206 | |
| B | GLY299 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22355528, ECO:0007744|PDB:3AU8 |
| Chain | Residue | Details |
| A | ASP231 | |
| A | GLU233 | |
| A | GLU315 | |
| B | ASP231 | |
| B | GLU233 | |
| B | GLU315 |
