6IXT
Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri in complex with NAD+ and Mg2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| A | 0006102 | biological_process | isocitrate metabolic process |
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| B | 0006102 | biological_process | isocitrate metabolic process |
| C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| C | 0006102 | biological_process | isocitrate metabolic process |
| D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| D | 0006102 | biological_process | isocitrate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | HIS339 |
| A | HOH682 |
| A | HOH708 |
| A | HOH744 |
| A | GLY340 |
| A | THR341 |
| A | VAL342 |
| A | ASP344 |
| A | MET345 |
| A | ASN358 |
| A | GOL503 |
| A | HOH613 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASP302 |
| A | ASP306 |
| A | HOH710 |
| B | ASP278 |
| B | HOH747 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLY316 |
| A | PHE317 |
| A | ASN358 |
| A | LEU360 |
| A | GLY361 |
| A | NAD501 |
| A | HOH613 |
| A | HOH637 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | GLY119 |
| A | ARG123 |
| A | HOH673 |
| A | HOH727 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | ASP380 |
| A | ARG381 |
| A | ASP382 |
| A | HOH696 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | TYR230 |
| B | TRP287 |
| B | GLN289 |
| B | GLY290 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | ASN118 |
| B | ARG122 |
| B | ARG152 |
| B | TYR159 |
| B | ASP302 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | HIS339 |
| B | GLY340 |
| B | THR341 |
| B | VAL342 |
| B | HOH784 |
| B | HOH785 |
| B | HOH786 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue NAD C 501 |
| Chain | Residue |
| C | HIS339 |
| C | GLY340 |
| C | THR341 |
| C | VAL342 |
| C | ASP344 |
| C | MET345 |
| C | LEU357 |
| C | ASN358 |
| C | HOH620 |
| C | HOH708 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | TYR230 |
| C | GLY290 |
| C | HOH770 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| C | ASP380 |
| C | ARG381 |
| C | ASP382 |
| C | HOH686 |
| C | HOH768 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| C | ASN118 |
| C | ARG122 |
| C | ARG152 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 501 |
| Chain | Residue |
| C | ASP278 |
| D | ARG132 |
| D | ASP302 |
| D | THR305 |
| D | ASP306 |
| D | SO4503 |
| D | HOH737 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | HIS339 |
| D | GLY340 |
| D | THR341 |
| D | VAL342 |
| D | HOH644 |
| D | HOH695 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 503 |
| Chain | Residue |
| C | LYS234 |
| D | ASN118 |
| D | ARG122 |
| D | ARG152 |
| D | TYR159 |
| D | ASP302 |
| D | GOL501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"6IXN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"7E2W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"6IXT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"6IXN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IXT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
