3AUA
Crystal structure of the quaternary complex-2 of an isomerase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| 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 | 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 | 30 |
| 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 | F98701 |
| A | HOH723 |
| A | HOH771 |
| A | HOH875 |
| A | HOH878 |
| A | GLY87 |
| A | HOH989 |
| 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 | F98701 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE F98 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 | HOH780 |
| A | HOH783 |
| site_id | AC4 |
| Number of Residues | 32 |
| 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 | F98702 |
| B | HOH720 |
| B | HOH751 |
| B | HOH759 |
| B | HOH826 |
| B | HOH840 |
| B | HOH841 |
| B | HOH921 |
| 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 | F98702 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE F98 B 702 |
| Chain | Residue |
| B | ILE302 |
| B | SER306 |
| B | ASN311 |
| B | LYS312 |
| B | GLU315 |
| B | NDP502 |
| B | MG602 |
| B | HOH755 |
| B | HOH883 |
| B | LYS205 |
| B | ASP231 |
| B | SER232 |
| B | GLU233 |
| B | SER269 |
| B | SER270 |
| B | GLY272 |
| B | HIS293 |
| B | TRP296 |
| B | MET298 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 489 |
| Chain | Residue |
| B | SER139 |
| B | GLU143 |
| B | HOH855 |
| B | HOH1049 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 490 |
| Chain | Residue |
| A | ASP242 |
| A | HOH871 |
| B | GLN239 |
| B | LEU241 |
| B | HOH761 |
| B | HOH770 |
| B | HOH811 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22355528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AU8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AUA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P45568","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22355528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AUA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22355528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AU8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
