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 | 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 |